%% This BibTeX bibliography file was created using BibDesk. %% http://bibdesk.sourceforge.net/ %% Created for Antonios Papaioannou at 2013-10-10 17:42:16 -0400 %% Saved with string encoding Unicode (UTF-8) @article{sun2011nmr, Author = {Sun, Cheng and Mitchell, Odingo and Huang, Jiaxin and Boutis, Gregory S}, Journal = {The Journal of Physical Chemistry B}, Number = {47}, Pages = {13935--13942}, Publisher = {ACS Publications}, Title = {NMR Studies of Localized Water and Protein Backbone Dynamics in Mechanically Strained Elastin}, Volume = {115}, Year = {2011}} @article{li2001hydrophobic, Author = {Li, Bin and Alonso, Darwin OV and Bennion, Brian J and Daggett, Valerie}, Journal = {Journal of the American Chemical Society}, Number = {48}, Pages = {11991--11998}, Publisher = {ACS Publications}, Title = {Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers}, Volume = {123}, Year = {2001}} @article{wasserman1990molecular, Author = {Wasserman, ZR and Salemme, FR}, Journal = {Biopolymers}, Number = {12-13}, Pages = {1613--1631}, Publisher = {Wiley Online Library}, Title = {A molecular dynamics investigation of the elastomeric restoring force in elastin}, Volume = {29}, Year = {1990}} @article{martin2012temperature, Author = {Mart{\'\i}n, Laura and Castro, Emilio and Ribeiro, Artur and Alonso, Matilde and Rodr{\'\i}guez-Cabello, J Carlos}, Journal = {Biomacromolecules}, Number = {2}, Pages = {293--298}, Publisher = {ACS Publications}, Title = {Temperature-triggered self-assembly of elastin-like block co-recombinamers: the controlled formation of micelles and vesicles in an aqueous medium}, Volume = {13}, Year = {2012}} @article{girotti2011elastin, Author = {Girotti, Alessandra and Fern{\'a}ndez-Colino, Alicia and L{\'o}pez, Isabel M and Rodr{\'\i}guez-Cabello, Jos{\'e} C and Arias, Francisco J}, Journal = {Biotechnology Journal}, Number = {10}, Pages = {1174--1186}, Publisher = {Wiley Online Library}, Title = {Elastin-like recombinamers: Biosynthetic strategies and biotechnological applications}, Volume = {6}, Year = {2011}} @article{reguera2007effect, Author = {Reguera, Javier and Urry, Dan W and Parker, Timothy M and McPherson, David T and Rodr{\'\i}guez-Cabello, J Carlos}, Journal = {Biomacromolecules}, Number = {2}, Pages = {354--358}, Publisher = {ACS Publications}, Title = {Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer}, Volume = {8}, Year = {2007}} @article{luan1991differential, Author = {Luan, Chi-Hao and Parker, Timothy M and Prasad, Kari U and Urry, Dan W}, Journal = {Biopolymers}, Number = {5}, Pages = {465--475}, Publisher = {Wiley Online Library}, Title = {Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin-based polytetra-, polypenta-, and polynonapeptides}, Volume = {31}, Year = {1991}} @article{serrano2007infrared, Author = {Serrano, Vesna and Liu, Wenge and Franzen, Stefan}, Date-Modified = {2013-10-10 21:39:04 +0000}, Journal = {Biophysical Journal}, Number = {7}, Pages = {2429--2435}, Publisher = {Elsevier}, Title = {An infrared spectroscopic study of the conformational transition of elastin-like polypeptides}, Volume = {93}, Year = {2007}} @article{meyer2004quantification, Author = {Meyer, Dan E and Chilkoti, Ashutosh}, Journal = {Biomacromolecules}, Number = {3}, Pages = {846--851}, Publisher = {ACS Publications}, Title = {Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides}, Volume = {5}, Year = {2004}} @article{wise2009engineered, Author = {Wise, Steven G and Mithieux, Suzanne M and Weiss, Anthony S}, Date-Modified = {2013-10-10 21:38:25 +0000}, Journal = {Advances in Protein Chemistry and Structural Biology}, Pages = {1--24}, Publisher = {Elsevier}, Title = {Engineered tropoelastin and elastin-based biomaterials}, Volume = {78}, Year = {2009}} @article{lillie1992effects, Author = {Lillie, MA and Gosline, JM}, Journal = {Biorheology}, Number = {3-4}, Pages = {229--242}, Title = {The effects of polar solutes on the viscoelastic behavior of elastin.}, Volume = {30}, Year = {1992}} @article{mistrali1971thermodynamics, Author = {Mistrali, F and Volpin, Dino and Garibaldo, GB and Ciferri, Alberto}, Date-Modified = {2013-10-10 21:40:49 +0000}, Journal = {The Journal of Physical Chemistry}, Number = {1}, Pages = {142--150}, Publisher = {ACS Publications}, Title = {Thermodynamics of elasticity in open systems. Elastin}, Volume = {75}, Year = {1971}} @article{sell2010use, Author = {Sell, Scott A and Wolfe, Patricia S and Garg, Koyal and McCool, Jennifer M and Rodriguez, Isaac A and Bowlin, Gary L}, Journal = {Polymers}, Number = {4}, Pages = {522--553}, Publisher = {Molecular Diversity Preservation International}, Title = {The use of natural polymers in tissue engineering: a focus on electrospun extracellular matrix analogues}, Volume = {2}, Year = {2010}} @article{kielty2006elastic, Author = {Kielty, Cay M}, Date-Modified = {2013-10-10 21:37:08 +0000}, Journal = {Expert Reviews in Molecular Medicine}, Number = {19}, Pages = {1--23}, Publisher = {Cambridge Univ Press}, Title = {Elastic fibres in health and disease}, Volume = {8}, Year = {2006}} @book{Abragam, Author = {Abragam, A.}, Month = Oct, Publisher = {Oxford University Press, USA}, Title = {{Principles of Nuclear Magnetism (International Series of Monographs on Physics)}}, Year = {1983}} @book{Duer, Author = {Duer, Melinda J.}, Month = Jul, Publisher = {Wiley-Blackwell, UK}, Title = {{Introduction to Solid-State NMR Spectroscopy}}, Year = {2005}} @book{Slichter, Author = {Slichter, C.P.}, Month = Mar, Publisher = {Springer, USA}, Title = {{Principles of Magnetic Resonance}}, Year = {1996}} @article{Kurbanov2011, Abstract = {The advantage of the solid state NMR for studying molecular dynamics is the capability to study slow motions without limitations: in the liquid state, if orienting media are not used, all anisotropic magnetic interactions are averaged out by fast overall Brownian tumbling of a molecule and thus investigation of slow internal conformational motions (e.g., of proteins) in solution can be conducted using only isotropic interactions. One of the main tools for obtaining amplitudes and correlation times of molecular motions in the $\mu$s time scale is measuring relaxation rate R(1)($\rho$). Yet, there have been a couple of unresolved problems in the quantitative analysis of the relaxation rates. First, when the resonance offset of the spin-lock pulse is used, the spin-lock field can be oriented under an arbitrary angle in respect to B(0). Second, the spin-lock frequency can be comparable or even less than the magic angle spinning rate. Up to now, there have been no equations for R(1)($\rho$) that would be applicable for any values of the spin-lock frequency, magic angle spinning rate and resonance offset of the spin-lock pulse. In this work such equations were derived for two most important relaxation mechanisms: heteronuclear dipolar coupling and chemical shift anisotropy. The validity of the equations was checked by numerical simulation of the R(1)($\rho$) experiment using SPINEVOLUTION program. In addition to that, the applicability of the well-known model-free approach to the solid state NMR relaxation data analysis was considered. For the wobbling in a cone at 30$\,^{\circ}$ and 90$\,^{\circ}$ cone angles and two-site jump models, it has been demonstrated that the auto-correlation functions G(0)(t), G(1)(t), G(2)(t), corresponding to different spherical harmonics, for isotropic samples (powders, polycrystals, etc.) are practically the same regardless of the correlation time of motion. This means that the model-free approach which is widely used in liquids can be equally applied, at least assuming these two motional models, to the analysis of the solid state NMR relaxation data.}, Author = {Kurbanov, Rauf and Zinkevich, Tatjana and Krushelnitsky, Alexey}, Doi = {10.1063/1.3658383}, File = {:Users/antonypapaioannou/Desktop/The nuclear magnetic resonance relaxation data analysis in solids.pdf:pdf}, Issn = {1089-7690}, Journal = {The Journal of Chemical Physics}, Keywords = {Magnetic Resonance Spectroscopy,Molecular Dynamics Simulation,Statistics as Topic}, Month = nov, Number = {18}, Pages = {184104}, Pmid = {22088049}, Title = {{The nuclear magnetic resonance relaxation data analysis in solids: general R1/R1($\rho$) equations and the model-free approach.}}, Volume = {135}, Year = {2011}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/22088049}, Bdsk-Url-2 = {http://dx.doi.org/10.1063/1.3658383}} @article{Lipari, Author = {Lipari, Giovanni and Szabo, Attila}, Doi = {10.1021/ja00381a009}, Eprint = {http://pubs.acs.org/doi/pdf/10.1021/ja00381a009}, Journal = {Journal of the American Chemical Society}, Number = {17}, Pages = {4546-4559}, Title = {Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity}, Volume = {104}, Year = {1982}, Bdsk-Url-1 = {http://pubs.acs.org/doi/abs/10.1021/ja00381a009}, Bdsk-Url-2 = {http://dx.doi.org/10.1021/ja00381a009}} @article{Clore1990, Author = {Clore, G. Marius and Szabo, Attila and Bax, Ad and Kay, Lewis E. and Driscoll, Paul C. and Gronenborn, Angela M.}, Doi = {10.1021/ja00168a070}, File = {:Users/antonypapaioannou/Downloads/deviations.pdf:pdf}, Issn = {0002-7863}, Journal = {Journal of the American Chemical Society}, Month = jun, Number = {12}, Pages = {4989--4991}, Title = {{Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins}}, Volume = {112}, Year = {1990}, Bdsk-Url-1 = {http://pubs.acs.org/doi/abs/10.1021/ja00168a070}, Bdsk-Url-2 = {http://dx.doi.org/10.1021/ja00168a070}} @article{Zhang2003, Abstract = {RefDB is a secondary database of reference-corrected protein chemical shifts derived from the BioMagResBank (BMRB). The database was assembled by using a recently developed program (SHIFTX) to predict protein (1)H, (13)C and (15)N chemical shifts from X-ray or NMR coordinate data of previously assigned proteins. The predicted shifts were then compared with the corresponding observed shifts and a variety of statistical evaluations performed. In this way, potential mis-assignments, typographical errors and chemical referencing errors could be identified and, in many cases, corrected. This approach allows for an unbiased, instrument-independent solution to the problem of retrospectively re-referencing published protein chemical shifts. Results from this study indicate that nearly 25\% of BMRB entries with (13)C protein assignments and 27\% of BMRB entries with (15)N protein assignments required significant chemical shift reference readjustments. Additionally, nearly 40\% of protein entries deposited in the BioMagResBank appear to have at least one assignment error. From this study it evident that protein NMR spectroscopists are increasingly adhering to recommended IUPAC (13)C and (15)N chemical shift referencing conventions, however, approximately 20\% of newly deposited protein entries in the BMRB are still being incorrectly referenced. This is cause for some concern. However, the utilization of RefDB and its companion programs may help mitigate this ongoing problem. RefDB is updated weekly and the database, along with its associated software, is freely available at http://redpoll.pharmacy.ualberta.ca and the BMRB website.}, Author = {Zhang, Haiyan and Neal, Stephen and Wishart, David S}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Zhang, Neal, Wishart - 2003 - RefDB a database of uniformly referenced protein chemical shifts.pdf:pdf}, Issn = {0925-2738}, Journal = {Journal of Biomolecular NMR}, Keywords = {Animals,Crystallography, X-Ray,Databases as Topic,Humans,Internet,Magnetic Resonance Spectroscopy,Models, Statistical,Protein Structure, Secondary,Proteins,Proteins: analysis,Proteins: chemistry,Software}, Month = mar, Number = {3}, Pages = {173--95}, Pmid = {12652131}, Title = {{RefDB: a database of uniformly referenced protein chemical shifts.}}, Volume = {25}, Year = {2003}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/12652131}} @article{Mecham2008, Abstract = {Elastin provides recoil to tissues subjected to repeated stretch, such as blood vessels and the lung. It is encoded by a single gene in mammals and is secreted as a 60-70 kDa monomer called tropoelastin. The functional form of the protein is that of a large, highly crosslinked polymer that organizes as sheets or fibers in the extracellular matrix. Purification of mature, crosslinked elastin is problematic because its insolubility precludes its isolation using standard wet-chemistry techniques. Instead, relatively harsh experimental approaches designed to remove non-elastin 'contaminates' are employed to generate an insoluble product that has the amino acid composition expected of elastin. Although soluble, tropoelastin also presents problems for isolation and purification. The protein's extreme stickiness and susceptibility to proteolysis requires careful attention during purification and in tropoelastin-based assays. This article describes the most common approaches for purification of insoluble elastin and tropoelastin. It also addresses key aspects of studying tropoelastin production in cultured cells, where elastin expression is highly dependent upon cell type, culture conditions, and passage number.}, Author = {Mecham, Robert P}, Doi = {10.1016/j.ymeth.2008.01.007}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Mecham - 2008 - Methods in elastic tissue biology elastin isolation and purification.pdf:pdf}, Issn = {1046-2023}, Journal = {Methods (San Diego, Calif.)}, Keywords = {Amino Acids,Amino Acids: chemistry,Animals,Cattle,Cells, Cultured,Desmosine,Desmosine: analysis,Desmosine: chemistry,Elastin,Elastin: chemistry,Elastin: isolation \& purification,Elastin: ultrastructure,Humans,Mice,Solubility}, Month = may, Number = {1}, Pages = {32--41}, Pmid = {18442703}, Title = {{Methods in elastic tissue biology: elastin isolation and purification.}}, Volume = {45}, Year = {2008}, Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2405817%5C&tool=pmcentrez%5C&rendertype=abstract}, Bdsk-Url-2 = {http://dx.doi.org/10.1016/j.ymeth.2008.01.007}} @article{Patrige1952, Author = {Partridge, S.M. and Davis, H.F. and Adair, S.T.}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Of, Acids - 1952 - The chemistry of connective tissues.pdf:pdf}, Journal = {Biochemical Journal}, Number = {1946}, Title = {{The Chemistry of Connective Tissues}}, Volume = {6}, Year = {1952}} @article{Lowry1941, Author = {Lowry, OH and Gilligan, DR and Katersky, EM}, File = {:Users/antonypapaioannou/Downloads/Lowry.pdf:pdf}, Journal = {Journal of Biological Chemistry}, Number = {2}, Title = {{The determination of collagen and elastin in tissues, with results obtained in various normal tissues from different species}}, Volume = {139}, Year = {1941}, Bdsk-Url-1 = {http://www.jbc.org/content/139/2/795.short}} @article{Starcher1976441, Author = {Barry C. Starcher and Michael J. Galione}, Doi = {10.1016/0003-2697(76)90224-4}, Issn = {0003-2697}, Journal = {Analytical Biochemistry}, Number = {2}, Pages = {441 - 447}, Title = {Purification and comparison of elastins from different animal species}, Volume = {74}, Year = {1976}, Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/pii/0003269776902244}, Bdsk-Url-2 = {http://dx.doi.org/10.1016/0003-2697(76)90224-4}} @article{Hong2003, Abstract = {The conformation of an elastin-mimetic recombinant protein, [(VPGVG)4(VPGKG)]39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and assign the isotropic chemical shifts of the various sites. The Pro 15N, 13Calpha, and 13Cbeta isotropic shifts, and the Gly-3 Calpha isotropic and anisotropic chemical shifts support the predominance of type-II beta-turn structure at the Pro-Gly pair but reject a type-I beta-turn. The Val-1 preceding Pro adopts mostly beta-sheet torsion angles, while the Val-4 chemical shifts are intermediate between those of helix and sheet. The protein exhibits a significant conformational distribution, shown by the broad line widths of the 15N and 13C spectra. The average chemical shifts of the solid protein are similar to the values in solution, suggesting that the low-hydration polypeptide maintains the same conformation as in solution. The ability to measure these conformational restraints by solid-state NMR opens the possibility of determining the detailed structure of this class of fibrous proteins through torsion angles and distances.}, Author = {Hong, M and Isailovic, D and McMillan, R a and Conticello, V P}, Doi = {10.1002/bip.10431}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Hong et al. - 2003 - Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.pdf:pdf}, Issn = {0006-3525}, Journal = {Biopolymers}, Keywords = {Amino Acid Motifs,Animals,Anisotropy,Elastin,Elastin: chemistry,Magnetic Resonance Spectroscopy,Magnetic Resonance Spectroscopy: methods,Peptides,Peptides: chemistry,Protein Conformation,Protein Structure, Secondary,Recombinant Proteins,Recombinant Proteins: chemistry}, Month = oct, Number = {2}, Pages = {158--68}, Pmid = {14517905}, Title = {{Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.}}, Volume = {70}, Year = {2003}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/14517905}, Bdsk-Url-2 = {http://dx.doi.org/10.1002/bip.10431}} @article{Perry2002, Abstract = {Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for elastin samples with different hydration levels. The spectral intensities in the aliphatic region undergo significant changes as 70\% of the water in hydrated elastin is removed. In addition, dramatic differences in the CPMAS spectra of hydrated, lyophilized, and partially dehydrated elastin samples over a relatively small temperature range (-20 degrees C to 37 degrees C) are observed. Results from other experiments, including (13)C T(1) and (1)H T(1 rho) measurements, direct polarization with magic-angle spinning, and static CP of the hydrated and lyophilized elastin preparations, also support the model that there is significant mobility in fully hydrated elastin. Our results support models in which water plays an integral role in the structure and proper function of elastin in vertebrate tissue.}, Author = {Perry, Ashlee and Stypa, Michael P and Tenn, Brandon K and Kumashiro, Kristin K}, Doi = {10.1016/S0006-3495(02)75468-4}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Perry et al. - 2002 - Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.pdf:pdf}, Issn = {0006-3495}, Journal = {Biophysical Journal}, Keywords = {Biophysical Phenomena,Biophysics,Carbon,Carbon: chemistry,Elastin,Elastin: chemistry,Hydrogen,Hydrogen: chemistry,Magnetic Resonance Spectroscopy,Magnetic Resonance Spectroscopy: methods,Structure-Activity Relationship,Temperature,Time Factors,Water,Water: chemistry,Water: metabolism}, Month = feb, Number = {2}, Pages = {1086--95}, Pmid = {11806948}, Publisher = {Elsevier}, Title = {{Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.}}, Volume = {82}, Year = {2002}, Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1301915%5C&tool=pmcentrez%5C&rendertype=abstract}, Bdsk-Url-2 = {http://dx.doi.org/10.1016/S0006-3495(02)75468-4}} @article{Debelle1999, Abstract = {Elastin, the protein responsible for the elastic properties of vertebrate tissues, has been thought to be solely restricted to that role. As a consequence, elastin was conventionally described as an amorphous polymer. Recent results in the biomedical, biochemical and biophysical fields have lead to the conclusion that the presence of elastin in the extracellular space has very complex implications involving many other molecules. The present review describes the current state of knowledge concerning elastin as an elastic macromolecule. First, the genetic, biological, biochemical and biophysical processes leading to a functional polymer are described. Second, the elastic function of elastin is discussed. The controversy on elastin structure and elasticity is discussed and a novel dynamic mechanism of elasticity proposed. Finally, pathologies where the elastin molecule is involved are considered. This updated description of functional elastin provides the required background for the understanding of its pathologies and defines clearly the properties a substance should possess to be qualified as a good elastic biomaterial.}, Author = {Debelle, L and Tamburro, A M}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Debelle, Tamburro - 1999 - Elastin molecular description and function.pdf:pdf}, Issn = {1357-2725}, Journal = {The International Journal of Biochemistry \& Cell Biology}, Keywords = {Animals,Aortic Valve Stenosis,Aortic Valve Stenosis: physiopathology,Cutis Laxa,Cutis Laxa: physiopathology,Elastic Tissue,Elastic Tissue: pathology,Elastin,Elastin: chemistry,Elastin: genetics,Elastin: metabolism,Humans,Skin Diseases,Skin Diseases: physiopathology,Structure-Activity Relationship,Williams Syndrome,Williams Syndrome: physiopathology}, Month = feb, Number = {2}, Pages = {261--72}, Pmid = {10216959}, Title = {{Elastin: molecular description and function.}}, Volume = {31}, Year = {1999}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10216959}} @article{Lillie2002, Abstract = {Purified aortic elastin displays failure behaviour characteristic of an amorphous, noncrystalizing elastomer with failure properties showing a strong dependence on viscoelastic behaviour. Tensile breaking stresses and breaking strains measured over a range of temperatures, hydration levels, and strain rates are reducible to single curves by the application of shift factors obtained from dynamic mechanical tests. The breaking stress of rubbery elastin is similar to that found in other elastomers, but glassy elastin is about an order of magnitude less strong than expected. We suggest elastin's ability to be strengthened through viscous dissipation of strain energy and crack tip blunting is limited by its fibrillar structure.}, Author = {Lillie, M A and Gosline, J M}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Lillie, Gosline - 2002 - The viscoelastic basis for the tensile strength of elastin.pdf:pdf}, Issn = {0141-8130}, Journal = {International Journal of Biological Macromolecules}, Keywords = {Animals,Aorta, Thoracic,Aorta, Thoracic: chemistry,Elastin,Elastin: chemistry,Swine,Tensile Strength}, Month = apr, Number = {2}, Pages = {119--27}, Pmid = {11911903}, Title = {{The viscoelastic basis for the tensile strength of elastin.}}, Volume = {30}, Year = {2002}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11911903}} @incollection{Urry2002, title={Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction}, author={Urry, DW and Parker, TM}, booktitle={Mechanics of Elastic Biomolecules}, pages={543--559}, year={2003}, publisher={Springer} } @article{Debelle2_1999, Abstract = {Elastin structures and their significance towards elastic recoil properties have been reviewed. Starting from the initial hypothesis that elastin conformation is conditioned by that of its monomer, the structure of tropoelastin was first described using theoretical and experimental methods and a beta class folding type was evidenced for the isolated unbound tropoelastin molecules. The structure of elastin in the solid state was consistent with that of its monomer and consequently, fibrous elastin appeared constituted of globular tropoelastin molecules. Finally, theoretical and experimental considerations have led us to the conclusion that the functional form of the elastomer, water swollen elastin, could be a triphasic system comprising the protein chains, hydration water and solvent water. Following this description, the dynamic structural equilibria occurring within elastin hydrophobic domains and the plasticizing effect of water could explain elastin elasticity, in keeping with a classical entropic mechanism.}, Author = {Debelle, L and Alix, A. J}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Debelle, Alix - 1999 - The structures of elastins and their function.pdf:pdf}, Issn = {0300-9084}, Journal = {Biochimie}, Keywords = {Amino Acid Sequence,Animals,Cattle,Chickens,Circular Dichroism,Elasticity,Elastin,Elastin: chemistry,Elastin: genetics,Humans,Mice,Models, Molecular,Molecular Sequence Data,Protein Conformation,Protein Folding,Protein Structure, Secondary,Rats,Sequence Homology, Amino Acid,Sheep,Spectroscopy, Fourier Transform Infrared,Tropoelastin,Tropoelastin: chemistry,Tropoelastin: genetics,Water,Water: chemistry}, Month = oct, Number = {10}, Pages = {981--94}, Pmid = {10575352}, Title = {{The structures of elastins and their function.}}, Volume = {81}, Year = {1999}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10575352}} @article{Li1997, Abstract = {Supravalvular aortic stenosis (SVAS) is an inherited obstructive vascular disease that affects the aorta, carotid, coronary and pulmonary arteries. Previous molecular genetic data have led to the hypothesis that SVAS results from mutations in the elastin gene, ELN. In these studies, the disease phenotype was linked to gross DNA rearrangements (35 and 85 kb deletions and a translocation) in three SVAS families. However, gross rearrangements of ELN have not been identified in most cases of autosomal dominant SVAS. To define the spectrum of ELN mutations responsible for this disorder, we refined the genomic structure of human ELN and used this information in mutational analyses. ELN point mutations co-segregate with the disease in four familial cases and are associated with SVAS in three sporadic cases. Two of the mutations are nonsense, one is a single base pair deletion and four are splice site mutations. In one sporadic case, the mutation arose de novo. These data demonstrate that point mutations of ELN cause autosomal dominant SVAS.}, Author = {Li, D Y and Toland, A E and Boak, B B and Atkinson, D L and Ensing, G J and Morris, C A and Keating, M T}, Date-Modified = {2013-10-10 21:03:14 +0000}, File = {:Users/antonypapaioannou/Downloads/Hum. Mol. Genet.-1997-Li-1021-8.pdf:pdf}, Issn = {0964-6906}, Journal = {Human Molecular Genetics}, Keywords = {Aortic Valve Stenosis,Aortic Valve Stenosis: genetics,Cloning, Molecular,DNA Mutational Analysis,DNA Primers,DNA Primers: genetics,Elastin,Elastin: genetics,Female,Frameshift Mutation,Humans,Male,Molecular Sequence Data,Mutation,Pedigree,Polymorphism, Single-Stranded Conformational,RNA Splicing}, Month = jul, Number = {7}, Pages = {1021--8}, Pmid = {9215670}, Title = {{Elastin point mutations cause an obstructive vascular disease, supravalvular aortic stenosis.}}, Volume = {6}, Year = {1997}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/9215670}} @article{Daamen2001, Author = {Daamen, W F and Hafmans, T and Veerkamp, J H and Kuppevelt, T H Van}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Daamen et al. - 2005 - Comparison of ve procedures for the puri cation of insoluble elastin.pdf:pdf}, Journal = {Biomaterials}, Keywords = {calci,cation,insoluble elastin,ligamentum nuchae,puri}, Number = {14}, Pages = {1997--2005}, Title = {{Comparison of five procedures for the purification of insoluble elastin}}, Volume = {22}, Year = {2001}} @article{Kumashiro2006, Abstract = {The principal protein component of the elastic fiber found in elastic tissues is elastin, an amorphous, cross-linked biopolymer that is assembled from a high molecular weight monomer. The hydrophobic and cross-linking domains of elastin have been considered separate and independent, such that changes to one region are not thought to affect the other. However, results from these solid-state 13C NMR experiments demonstrate that cooperativity in protein folding exists between the two domain types. The sequence of the EP20-24-24 polypeptide has three hydrophobic sequences from exons 20 and 24 of the soluble monomer tropoelastin, interspersed with cross-linking domains constructed from exons 21 and 23. In the middle of each cross-linking domain is a "hinge" sequence. When this pentapeptide is replaced with alanines, as in EP20-24-24[23U], its properties are changed. In addition to the expected increase in alpha-helical content and the resulting increase in rigidity of the cross-linking domains, changes to the organization of the hydrophobic regions are also observed. Using one-dimensional CPMAS (cross-polarization with magic angle spinning) techniques, including spectral editing and relaxation measurements, evidence for a change in dynamics to both domain types is observed. Furthermore, it is likely that the methyl groups of the leucines of the hydrophobic domains are also affected by the substitution to the hinge region of the cross-linking sequences. This cooperativity between the two domain types brings new questions to the phenomenon of coacervation in elastin polypeptides and strongly suggests that functional models for the protein must include a role for the cross-linking regions.}, Author = {Kumashiro, Kristin K and Ho, Joanna P and Niemczura, Walter P and Keeley, Fred W}, Doi = {10.1074/jbc.M510833200}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Kumashiro et al. - 2006 - Cooperativity between the hydrophobic and cross-linking domains of elastin.pdf:pdf}, Issn = {0021-9258}, Journal = {The Journal of Biological Chemistry}, Keywords = {Alanine,Alanine: chemistry,Amino Acid Sequence,Amino Acid Substitution,Carbon Isotopes,Carbon Isotopes: chemistry,Elastin,Elastin: chemistry,Humans,Hydrophobic and Hydrophilic Interactions,Magnetic Resonance Spectroscopy,Molecular Sequence Data,Peptides,Peptides: chemistry,Protein Structure, Secondary,Protein Structure, Tertiary,Recombinant Proteins,Recombinant Proteins: chemistry,Repetitive Sequences, Amino Acid,Structure-Activity Relationship}, Month = aug, Number = {33}, Pages = {23757--65}, Pmid = {16777851}, Title = {{Cooperativity between the hydrophobic and cross-linking domains of elastin.}}, Volume = {281}, Year = {2006}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16777851}, Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M510833200}} @article{Pometun2004, Abstract = {Elastin is a key protein in soft tissue function and pathology. Establishing a structural basis for understanding its reversible elasticity has proven to be difficult. Complementary to structure is the important aspect of flexibility and disorder in elastin. We have used solid-state NMR methods to examine polypeptide and hydrate ordering in both elastic (hydrated) and brittle (dry) elastin fibers and conclude (i) that tightly bound waters are absent in both dry and hydrated elastin and (ii) that the backbone in the hydrated protein is highly disordered with large amplitude motions. The hydrate was studied by (2)H and (17)O NMR, and the polypeptide by (13)C and (2)H NMR. Using a two-dimensional (13)C MAS method, an upper limit of S < 0.1 was determined for the backbone carbonyl group order parameter in hydrated elastin. For comparison, S approximately approximately 0.9 in most proteins. The former result is substantiated by two additional observations: the absence of the characteristic (2)H spectrum for stationary amides and "solution-like" (13)C magic angle spinning spectra at 75 degrees C, at which the material retains elasticity. Comparison of the observed shifts with accepted values for alpha-helices, beta-sheets, or random coils indicates a random coil structure at all carbons. These conclusions are discussed in the context of known thermodynamic properties of elastin and, more generally, protein folding. Because coacervation is an entropy-driven process, it is enhanced by the observed backbone disorder, which, we suggest, is the result of high proline content. This view is supported by recent studies of recombinant elastin polypeptides with systematic proline substitutions.}, Author = {Pometun, Maxim S and Chekmenev, Eduard Y and Wittebort, Richard J}, Doi = {10.1074/jbc.M310948200}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Pometun, Chekmenev, Wittebort - 2004 - Quantitative observation of backbone disorder in native elastin.pdf:pdf}, Isbn = {5028526613}, Issn = {0021-9258}, Journal = {The Journal of Biological Chemistry}, Keywords = {Animals,Cattle,Chemistry, Physical,Deuterium,Elasticity,Elastin,Elastin: chemistry,Magnetic Resonance Spectroscopy,Physicochemical Phenomena,Proline,Proline: analysis,Protein Structure, Secondary,Spectrum Analysis,Thermodynamics,Water,Water: chemistry}, Month = mar, Number = {9}, Pages = {7982--7}, Pmid = {14625282}, Title = {{Quantitative observation of backbone disorder in native elastin.}}, Volume = {279}, Year = {2004}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/14625282}, Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M310948200}} @article{Wang2002, Author = {Wang, Yunjun and Jardetzky, Oleg}, Doi = {10.1110/ps.3180102.Structure}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Wang, Jardetzky - 2002 - Probability-based protein secondary structure identification using combined NMR chemical-shift data.pdf:pdf}, Journal = {Protein Science}, Keywords = {1967,al-,been,chemical shift,known to have a,markley et al,nakamura and jardetzky 1968,nmr,nmr chemical shifts have,protein secondary structure,s,secondary structure identification,since the late 1960,strong correlation with secondary,structure}, Number = {4}, Pages = {852--861}, Title = {{Probability-based protein secondary structure identification using combined NMR chemical-shift data}}, Volume = {11}, Year = {2002}, Bdsk-Url-1 = {http://onlinelibrary.wiley.com/doi/10.1110/ps.3180102/full}, Bdsk-Url-2 = {http://dx.doi.org/10.1110/ps.3180102.Structure}} @article{Kumashiro2001, Abstract = {High-resolution solid-state (13)C NMR spectra are presented for samples of alpha-elastin prepared from the aorta of normal and copper-deficient pigs. Chemical shifts of the various peaks indicate that both the normal and undercross-linked peptides have similar overall structures. However, (13)C T(1), (13)C T(1 rho), and (1)H T(1 rho) measurements indicate that the alpha-elastin peptides obtained from the abnormal elastic fibers samples exhibit altered mobilities, particularly in their side chains. Results from spectra taken with a range of contact times and from dipolar dephasing experiments are consistent with conclusions reached with the relaxation measurements. Namely, the loss of function associated with the undercross-linked sample is correlated to a small but measurable difference in relative mobility.}, Author = {Kumashiro, K K and Kim, M S and Kaczmarek, S E and Sandberg, L B and Boyd, C D}, Doi = {10.1002/1097-0282(20011005)59:4<266::AID-BIP1023>3.0.CO;2-2}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Kumashiro et al. - 2001 - (13)C cross-polarizationmagic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links.pdf:pdf}, Issn = {0006-3525}, Journal = {Biopolymers}, Keywords = {Animals,Biopolymers,Biopolymers: chemistry,Biopolymers: isolation \& purification,Carbon Isotopes,Copper,Copper: deficiency,Cross-Linking Reagents,Elastin,Elastin: chemistry,Elastin: isolation \& purification,Magnetic Resonance Spectroscopy,Swine}, Month = oct, Number = {4}, Pages = {266--75}, Pmid = {11473351}, Title = {{(13)C cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links.}}, Volume = {59}, Year = {2001}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11473351}, Bdsk-Url-2 = {http://dx.doi.org/10.1002/1097-0282(20011005)59:4%3C266::AID-BIP1023%3E3.0.CO;2-2}} @article{Asakura1999, Abstract = {The polymorphic structures of silk fibroins in the solid state were examined on the basis of a quantitative relationship between the 13C chemical shift and local structure in proteins. To determine this relationship, 13C chemical shift contour plots for C alpha and C beta carbons of Ala and Ser residues, and the C alpha chemical shift plot for Gly residues were prepared using atomic co-ordinates from the Protein Data Bank and 13C NMR chemical shift data in aqueous solution reported for 40 proteins. The 13C CP/MAS NMR chemical shifts of Ala, Ser and Gly residues of Bombyx mori silk fibroin in silk I and silk II forms were used along with 13C CP/MAS NMR chemical shifts of Ala residues of Samia cynthia ricini silk fibroin in beta-sheet and alpha-helix forms for the structure analyses of silk fibroins. The allowed regions in the 13C chemical shift contour plots for C alpha and C beta carbons of Ala and Ser residues for the structures in silk fibroins, i.e. Silk II, Silk I and alpha-helix, were determined using their 13C isotropic NMR chemical shifts in the solid state. There are two area of the phi,psi map which satisfy the observed Silk I chemical shift data for both the C alpha and C beta carbons of Ala and Ser residues in the 13C chemical shift contour plots.}, Author = {Asakura, T and Iwadate, M and Demura, M and Williamson, M P}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Asakura et al. - 1999 - Structural analysis of silk with 13C NMR chemical shift contour plots.pdf:pdf}, Issn = {0141-8130}, Journal = {International Journal of Biological Macromolecules}, Keywords = {Alanine,Alanine: chemistry,Amino Acids,Amino Acids: chemistry,Animals,Bombyx,Bombyx: chemistry,Databases, Factual,Glycine,Glycine: chemistry,Insect Proteins,Insect Proteins: chemistry,Magnetic Resonance Spectroscopy,Magnetic Resonance Spectroscopy: methods,Protein Conformation,Serine,Serine: chemistry,Silk}, Number = {2-3}, Pages = {167--71}, Pmid = {10342761}, Title = {{Structural analysis of silk with 13C NMR chemical shift contour plots.}}, Volume = {24}, Year = {1999}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10342761}} @article{Jenkins2010, Abstract = {Synthetic spider silk holds great potential for use in various applications spanning medical uses to ultra lightweight armor; however, producing synthetic fibers with mechanical properties comparable to natural spider silk has eluded the scientific community. Natural dragline spider silks are commonly made from proteins that contain highly repetitive amino acid motifs, adopting an array of secondary structures. Before further advances can be made in the production of synthetic fibers based on spider silk proteins, it is imperative to know the percentage of each amino acid in the protein that forms a specific secondary structure. Linking these percentages to the primary amino acid sequence of the protein will establish a structural foundation for synthetic silk. In this study, nuclear magnetic resonance (NMR) techniques are used to quantify the percentage of Ala, Gly, and Ser that form both beta-sheet and helical secondary structures. The fraction of these three amino acids and their secondary structure are quantitatively correlated to the primary amino acid sequence for the proteins that comprise major and minor ampullate silk from the Nephila clavipes spider providing a blueprint for synthetic spider silks.}, Author = {Jenkins, Janelle E and Creager, Melinda S and Lewis, Randolph V and Holland, Gregory P and Yarger, Jeffery L}, Doi = {10.1021/bm9010672}, File = {:Users/antonypapaioannou/Downloads/Quantitative Correlation between the Protein Primary Sequences and Secondary Structures in Spider Dragline Silks.pdf:pdf}, Issn = {1526-4602}, Journal = {Biomacromolecules}, Keywords = {Amino Acid Sequence,Animals,Fibroins,Fibroins: chemistry,Molecular Sequence Data,Nuclear Magnetic Resonance, Biomolecular,Protein Structure, Secondary,Silk,Silk: chemistry,Spiders,X-Ray Diffraction}, Month = jan, Number = {1}, Pages = {192--200}, Pmid = {20000730}, Title = {{Quantitative Correlation between the protein primary sequences and secondary structures in spider dragline silks.}}, Volume = {11}, Year = {2010}, Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2805410%5C&tool=pmcentrez%5C&rendertype=abstract}, Bdsk-Url-2 = {http://dx.doi.org/10.1021/bm9010672}} @article{Bennett1995, Author = {Bennett, Andrew E. and Rienstra, Chad M. and Auger, Michele and Lakshmi, K. V. and Griffin, Robert G.}, Doi = {10.1063/1.470372}, File = {:Users/antonypapaioannou/Downloads/Heteronuclear decoupling in rotating solids.pdf:pdf}, Issn = {00219606}, Journal = {The Journal of Chemical Physics}, Number = {16}, Pages = {6951}, Title = {{Heteronuclear decoupling in rotating solids}}, Volume = {103}, Year = {1995}, Bdsk-Url-1 = {http://link.aip.org/link/JCPSA6/v103/i16/p6951/s1%5C&Agg=doi}, Bdsk-Url-2 = {http://dx.doi.org/10.1063/1.470372}} @article{Yao2004, Abstract = {Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic protein as a function of hydration to better understand the origin of elastin elasticity. Poly(Lys-25), [(VPGVG)(4)(VPGKG)](39), has a repeat sequence common to natural elastin. (13)C cross-polarization and direct polarization spectra at various hydration levels indicate that water enhances the protein motion in a non-uniform manner. Below 20\% hydration, the backbone motion increases only slightly whereas above 30\% hydration, both the backbone and the side-chains undergo large-amplitude motions. The motional amplitudes are extracted from (13)C-(1)H and (1)H-(1)H dipolar couplings using 2D isotropic-anisotropic correlation experiments. The root mean square fluctuation angles are found to be 11-18 degrees in the dry protein and 16-21 degrees in the 20\% hydrated protein. Dramatically, the amplitudes increase to near isotropic at 30\% hydration. Field-dependent (1)H rotating-frame spin-lattice relaxation times (T(1rho)) indicate that significant motions occur on the microsecond time-scale (1.2-2.3 micros). The large-amplitude and low-frequency motion of poly(Lys-25) at relatively mild hydration indicates that the conformational entropy of the protein in the relaxed state contributes significantly to the elasticity.}, Author = {Yao, Xiao L and Conticello, Vincent P and Hong, Mei}, Doi = {10.1002/mrc.1330}, File = {:Users/antonypapaioannou/Downloads/investigation.pdf:pdf}, Issn = {0749-1581}, Journal = {Magnetic Resonance in Chemistry}, Keywords = {Amino Acid Sequence,Carbon Isotopes,Elastin,Elastin: chemistry,Hydrogen,Kinetics,Magnetic Resonance Spectroscopy,Magnetic Resonance Spectroscopy: methods,Molecular Sequence Data,Peptide Fragments,Peptide Fragments: chemistry,Peptides,Peptides: chemistry,Polylysine,Polylysine: chemistry,Protein Conformation}, Month = feb, Number = {2}, Pages = {267--75}, Pmid = {14745807}, Title = {{Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.}}, Volume = {42}, Year = {2004}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/14745807}, Bdsk-Url-2 = {http://dx.doi.org/10.1002/mrc.1330}} @article{Sun2011, Abstract = {We report on measurements of the dynamics of localized waters of hydration and the protein backbone of elastin, a remarkable resilient protein found in vertebrate tissues, as a function of the applied external strain. Using deuterium 2D T(1)-T(2) NMR, we separate four reservoirs in the elastin-water system characterized by water with distinguishable mobilities. The measured correlation times corresponding to random tumbling of water localized to the protein is observed to decrease with increasing strain and is interpreted as an increase in its orientational entropy. The NMR T(1) and T(1$\rho$) relaxation times of the carbonyl and aliphatic carbons of the protein backbone are measured and indicate a reduction in the correlation time as the elastomer strain is increased. It is argued, and supported by MD simulation of a short model elastin peptide [VPGVG](3), that the observed changes in the backbone dynamics give rise to the development of an entropic elastomeric force that is responsible for elastins' remarkable elasticity.}, Author = {Sun, Cheng and Mitchell, Odingo and Huang, Jiaxin and Boutis, Gregory S}, Doi = {10.1021/jp207607r}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Sun et al. - 2011 - NMR studies of localized water and protein backbone dynamics in mechanically strained elastin.pdf:pdf}, Issn = {1520-5207}, Journal = {The Journal of Physical Chemistry B}, Month = dec, Number = {47}, Pages = {13935--42}, Pmid = {22017547}, Title = {{NMR studies of localized water and protein backbone dynamics in mechanically strained elastin.}}, Volume = {115}, Year = {2011}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/22017547}, Bdsk-Url-2 = {http://dx.doi.org/10.1021/jp207607r}} @article{Urry1985, Abstract = {Carbon-13 NMR longitudinal relaxation time and line-width studies are reported on the coacervate concentration (about 60\% water by weight) of singly carbonyl carbon enriched polypentapeptides of elastin: specifically, (L-Val1-L-[1-13C]Pro2-Gly3-L-Val4-Gly5)n and (L-Val1-L-Pro2-Gly3-L-Val4-[1-13C]Gly5)n. On raising the temperature from 10 to 25 degrees C and from 40 to 70 degrees C, carbonyl mobility increases, but over the temperature interval from 25 to 40 degrees C, the mobility decreases. The results characterize an inverse temperature transition in the most fundamental sense of temperature being a measure of molecular motion. This transition in the state of the polypentapeptide indicates an increase in order of polypeptide on raising the temperature from 25 degrees C to physiological temperature. This fundamental NMR characterization corresponds with the results of numerous other physical methods, e.g., circular dichroism, dielectric relaxation, and electron microscopy, that correspondingly indicate an increase in order of the polypentapeptide both intramolecularly and intermolecularly for the same temperature increase from 25 to 40 degrees C. Significantly with respect to elastomeric function, thermoelasticity studies on gamma-irradiation cross-linked polypentapeptide coacervate show a dramatic increase in elastomeric force over the same interval that is here characterized by NMR as an inverse temperature transition. The temperature dependence of mobility above 40 degrees C indicates an activation energy of the order of 1.2 kcal/mol, which is the magnitude of barrier expected for elasticity.}, Author = {Urry, D W and Trapane, T L and Iqbal, M and Venkatachalam, C M and Prasad, K U}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Urry et al. - 1985 - Carbon-13 NMR relaxation studies demonstrate an inverse temperature transition in the elastin polypentapeptide.pdf:pdf}, Issn = {0006-2960}, Journal = {Biochemistry}, Keywords = {Amino Acid Sequence,Elastin,Kinetics,Magnetic Resonance Spectroscopy,Magnetic Resonance Spectroscopy: methods,Peptides,Thermodynamics}, Month = sep, Number = {19}, Pages = {5182--9}, Pmid = {4074687}, Title = {{Carbon-13 NMR relaxation studies demonstrate an inverse temperature transition in the elastin polypentapeptide.}}, Volume = {24}, Year = {1985}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/4074687}} @article{Urry1975, Author = {Urry, D W and Mitchell, L W and Ohnishi, T and Long, M M}, File = {:Users/antonypapaioannou/Downloads/Proton and Carbon Magnetic Resonance Studies of the Synthetic Polypentapeptide of Elastin.pdf:pdf}, Issn = {0022-2836}, Journal = {Journal of Molecular Biology}, Keywords = {Amino Acids,Amino Acids: analysis,Carbon Isotopes,Elastin,Hydrogen Bonding,Magnetic Resonance Spectroscopy,Mathematics,Models, Molecular,Oligopeptides,Oligopeptides: chemical synthesis,Peptides,Protein Conformation}, Month = jul, Number = {1}, Pages = {101--17}, Pmid = {1159785}, Title = {{Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin.}}, Volume = {96}, Year = {1975}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/1159785}} @article{Gray1973, Author = {Gray, WR}, File = {:Users/antonypapaioannou/Downloads/molecular model of elastin structure and function.pdf:pdf}, Journal = {Nature}, Number = {5434}, Pages = {461--466}, Title = {{Molecular model of elastin structure and function}}, Volume = {246}, Year = {1973}, Bdsk-Url-1 = {http://adsabs.harvard.edu/abs/1973Natur.246..461G}} @article{Christensen2013, Abstract = {Elastin-like polypeptides (ELPs) are thermally sensitive peptide polymers that undergo thermally triggered phase separation and this behavior is imparted to soluble proteins when they are fused to an ELP. The transition temperature of the ELP fusion protein is observed to be different than that of a free ELP, indicating that the surface properties of the fused protein modulate the thermal behavior of ELPs. Understanding this effect is important for the rational design of applications that exploit the phase transition behavior of ELP fusion proteins. We had previously developed a biophysical model that explained the effect of hydrophobic proteins on depressing the transition temperature of ELP fusion proteins relative to free ELP. Here, we extend the model to elucidate the effect of hydrophilic proteins on the thermal behavior of ELP fusion proteins. A linear correlation was found between overall residue composition of accessible protein surface weighted by a characteristic transition temperature for each residue and the difference in transition temperatures between the ELP protein fusion and the corresponding free ELP. In breaking down the contribution of residues to polar, nonpolar, and charged, the model revealed that charged residues are the most important parameter in altering the transition temperature of an ELP fusion relative to the free ELP.}, Author = {Christensen, Trine and Hassouneh, Wafa and Trabbic-Carlson, Kimberley and Chilkoti, Ashutosh}, Doi = {10.1021/bm400167h}, File = {:Users/antonypapaioannou/Downloads/Predicting Transition Temperatures of Elastin-Like Polypeptide Fusion Proteins.pdf:pdf}, Issn = {1526-4602}, Journal = {Biomacromolecules}, Month = may, Number = {5}, Pages = {1514--9}, Pmid = {23565607}, Title = {{Predicting transition temperatures of elastin-like polypeptide fusion proteins.}}, Volume = {14}, Year = {2013}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/23565607}, Bdsk-Url-2 = {http://dx.doi.org/10.1021/bm400167h}} @article{Li2001, Abstract = {Elastin undergoes an "inverse temperature transition" such that it becomes more ordered as the temperature increases. To investigate the molecular basis for this behavior, molecular dynamics simulations were conducted above and below the transition temperature. Simulations of a 90-residue elastin peptide, (VPGVG)(18), with explicit water molecules were performed at seven different temperatures between 7 and 42 degrees C, for a total of 80 ns. Beginning from an idealized beta-spiral structure, hydrophobic collapse was observed over a narrow temperature range in the simulations. Moreover, simulations above and below elastin's transition temperature indicate that elastin has more turns and distorted beta-structure at higher temperatures. Water was critical to the inverse temperature transition and elastin-associated water molecules can be divided into three categories: those closely associated with beta II turns; those that form hydrogen bonds with the main-chain groups; and those hydrating the hydrophobic side-chains. Water-swollen, monomeric elastin above the transition temperature is best described as a compact amorphous structure with distorted beta-strands, fluctuating turns, buried hydrophobic residues, and main-chain polar atoms that participate in hydrogen bonds with water. Below the transition temperature, elastin is expanded with approximately 40 \% local beta-spiral structure. Overall the simulations are in agreement with experiment and therefore appear to provide an atomic-level description of the conformational properties of elastin monomers and the basis for their elastomeric properties.}, Author = {Li, B and Alonso, D O and Daggett, V}, Doi = {10.1006/jmbi.2000.4306}, File = {:Users/antonypapaioannou/Library/Application Support/Mendeley Desktop/Downloaded/Li, Alonso, Daggett - 2001 - The molecular basis for the inverse temperature transition of elastin(2).pdf:pdf}, Issn = {0022-2836}, Journal = {Journal of Molecular Biology}, Keywords = {Amino Acid Sequence,Computer Simulation,Elasticity,Elastin,Elastin: chemistry,Elastin: metabolism,Hydrogen Bonding,Models, Molecular,Peptide Fragments,Peptide Fragments: chemistry,Peptide Fragments: metabolism,Protein Structure, Secondary,Temperature,Water,Water: metabolism}, Month = jan, Number = {3}, Pages = {581--92}, Pmid = {11152614}, Title = {{The molecular basis for the inverse temperature transition of elastin.}}, Volume = {305}, Year = {2001}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11152614}, Bdsk-Url-2 = {http://dx.doi.org/10.1006/jmbi.2000.4306}} @article{Glycines, Abstract = {We report the solid-state 13C and 15N NMR of insoluble elastin which has been synthesized in vitro with isotopically enriched glycine. Most of the glycines reside in a domain with good cross-polarization (CP) efficiencies, although surprisingly, a portion resides in an environment that is not detectable using CP. Our data indicate that much of the 13C population resides in regions of significant conformational flexibility. To support these conclusions, we present 13C and 15N cross-polarization with magic-angle-spinning (CPMAS) data in conjunction with "direct-polarization", nonspinning CP, and T1 measurements.}, Author = {Perry, Ashlee and Stypa, Michael P and Foster, Judith a and Kumashiro, Kristin K}, File = {:Users/antonypapaioannou/Downloads/Observation of the Glycines in Elastin Using 13C and 15N Solid-State NMR Spectroscopy and Isotopic Labeling.pdf:pdf}, Issn = {0002-7863}, Journal = {Journal of the American Chemical Society}, Keywords = {Animals,Carbon Isotopes,Cells, Cultured,Elastin,Elastin: biosynthesis,Elastin: chemistry,Glycine,Glycine: chemistry,Isotope Labeling,Muscle, Smooth,Muscle, Smooth: chemistry,Muscle, Smooth: metabolism,Nitrogen Isotopes,Nuclear Magnetic Resonance, Biomolecular,Rats,Rats, Sprague-Dawley}, Month = jun, Number = {24}, Pages = {6832--3}, Pmid = {12059197}, Title = {{Observation of the glycines in elastin using (13)C and (15)N solid-state NMR spectroscopy and isotopic labeling.}}, Volume = {124}, Year = {2002}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/12059197}} @inproceedings{gotte1968some, Author = {Gotte, L and Mammi, M and Pezzin, G}, Booktitle = {Symposium on Fibrous Proteins. Butterworths, Sydney, Australia}, Pages = {236--245}, Title = {Some structural aspects of elastin revealed by X-ray diffraction and other physical methods}, Year = {1968}} @article{Frushour1975, Author = {Frushour, B G and Koenig, J L}, Doi = {10.1002/bip.1975.360140211}, File = {:Users/antonypapaioannou/Downloads/Raman scattering of collagen, gelatin, and elastin.pdf:pdf}, Issn = {0006-3525}, Journal = {Biopolymers}, Keywords = {Achilles Tendon,Amides,Amino Acids,Animals,Cattle,Collagen,Elastin,Gelatin,Skin,Spectrum Analysis,Spectrum Analysis: methods,Tropocollagen}, Month = feb, Number = {2}, Pages = {379--91}, Pmid = {1174668}, Title = {{Raman scattering of collagen, gelatin, and elastin.}}, Volume = {14}, Year = {1975}, Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/1174668}, Bdsk-Url-2 = {http://dx.doi.org/10.1002/bip.1975.360140211}} @article{Gosline1975, Author = {Gosline, John M. and Yew, Foch F. and Weis-Fogh, Torkel}, Doi = {10.1002/bip.1975.360140904}, File = {:Users/antonypapaioannou/Downloads/Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluores- cence probe analysis.pdf:pdf}, Issn = {0006-3525}, Journal = {Biopolymers}, Month = sep, Number = {9}, Pages = {1811--1826}, Title = {{Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis}}, Volume = {14}, Year = {1975}, Bdsk-Url-1 = {http://doi.wiley.com/10.1002/bip.1975.360140904}, Bdsk-Url-2 = {http://dx.doi.org/10.1002/bip.1975.360140904}} @article{Mammi1968, Author = {Mammi, M and Gotte, L and Pezzin, G}, File = {:Users/antonypapaioannou/Downloads/Evidence for order in the structure of a-elastin.pdf:pdf}, Journal = {Nature}, Number = {5165}, Pages = {371--373}, Title = {{Evidence for order in the structure of $\alpha$-elastin}}, Volume = {220}, Year = {1968}, Bdsk-Url-1 = {http://www.nature.com/nature/journal/v220/n5165/abs/220371b0.html}} @article{Abatangelo1973, Author = {Abatangelo, G and Daga-Gordini, D and Tamburro, A. M.}, File = {:Users/antonypapaioannou/Downloads/SOLUBLE FRAGMENTS OF ELASTIN. CIRCULAR DICHROISM STUDIES.pdf:pdf}, Journal = {International Journal of Peptide and Protein Research}, Number = {2}, Pages = {63--68}, Title = {{Soluble fragments of elastin. Circular Dichroism studies}}, Volume = {5}, Year = {1973}, Bdsk-Url-1 = {http://onlinelibrary.wiley.com/doi/10.1111/j.1399-3011.1973.tb02319.x/abstract}} @article{Lusceac2010, Author = {Lusceac, Sorin A and Vogel, Michael R and Herbers, Claudia R}, Journal = {Biochimica et Biophysica acta. 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