Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1996 Jun 11;93(12):5680–5681. doi: 10.1073/pnas.93.12.5680

Protein minimization: downsizing through mutation.

W F DeGrado 1, T R Sosnick 1
PMCID: PMC39119  PMID: 8650151

Full text

PDF
5680

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Braisted A. C., Wells J. A. Minimizing a binding domain from protein A. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):5688–5692. doi: 10.1073/pnas.93.12.5688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cordes M. H., Davidson A. R., Sauer R. T. Sequence space, folding and protein design. Curr Opin Struct Biol. 1996 Feb;6(1):3–10. doi: 10.1016/s0959-440x(96)80088-1. [DOI] [PubMed] [Google Scholar]
  3. Fezoui Y., Weaver D. L., Osterhout J. J. De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3675–3679. doi: 10.1073/pnas.91.9.3675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gallop M. A., Barrett R. W., Dower W. J., Fodor S. P., Gordon E. M. Applications of combinatorial technologies to drug discovery. 1. Background and peptide combinatorial libraries. J Med Chem. 1994 Apr 29;37(9):1233–1251. doi: 10.1021/jm00035a001. [DOI] [PubMed] [Google Scholar]
  5. Jendeberg L., Persson B., Andersson R., Karlsson R., Uhlén M., Nilsson B. Kinetic analysis of the interaction between protein A domain variants and human Fc using plasmon resonance detection. J Mol Recognit. 1995 Jul-Aug;8(4):270–278. doi: 10.1002/jmr.300080405. [DOI] [PubMed] [Google Scholar]
  6. Krylov D., Mikhailenko I., Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 1994 Jun 15;13(12):2849–2861. doi: 10.1002/j.1460-2075.1994.tb06579.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kuroda Y., Nakai T., Ohkubo T. Solution structure of a de novo helical protein by 2D-NMR spectroscopy. J Mol Biol. 1994 Feb 25;236(3):862–868. doi: 10.1006/jmbi.1994.1194. [DOI] [PubMed] [Google Scholar]
  8. Lumb K. J., Carr C. M., Kim P. S. Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4. Biochemistry. 1994 Jun 14;33(23):7361–7367. doi: 10.1021/bi00189a042. [DOI] [PubMed] [Google Scholar]
  9. Lumb K. J., Kim P. S. A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry. 1995 Jul 11;34(27):8642–8648. doi: 10.1021/bi00027a013. [DOI] [PubMed] [Google Scholar]
  10. Lumb K. J., Kim P. S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 1995 Apr 21;268(5209):436–439. doi: 10.1126/science.7716550. [DOI] [PubMed] [Google Scholar]
  11. Myszka D. G., Chaiken I. M. Design and characterization of an intramolecular antiparallel coiled coil peptide. Biochemistry. 1994 Mar 8;33(9):2363–2372. doi: 10.1021/bi00175a003. [DOI] [PubMed] [Google Scholar]
  12. O'Neil K. T., Hoess R. H. Phage display: protein engineering by directed evolution. Curr Opin Struct Biol. 1995 Aug;5(4):443–449. doi: 10.1016/0959-440x(95)80027-1. [DOI] [PubMed] [Google Scholar]
  13. Struthers M. D., Cheng R. P., Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science. 1996 Jan 19;271(5247):342–345. doi: 10.1126/science.271.5247.342. [DOI] [PubMed] [Google Scholar]
  14. Tashiro M., Montelione G. T. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins. Curr Opin Struct Biol. 1995 Aug;5(4):471–481. doi: 10.1016/0959-440x(95)80031-x. [DOI] [PubMed] [Google Scholar]
  15. Yu Y., Monera O. D., Hodges R. S., Privalov P. L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J Mol Biol. 1996 Jan 26;255(3):367–372. doi: 10.1006/jmbi.1996.0030. [DOI] [PubMed] [Google Scholar]
  16. Zhou H. X., Hoess R. H., DeGrado W. F. In vitro evolution of thermodynamically stable turns. Nat Struct Biol. 1996 May;3(5):446–451. doi: 10.1038/nsb0596-446. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES