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
. 1982 Nov;79(22):7047–7051. doi: 10.1073/pnas.79.22.7047

Origin of the right-handed twist of beta-sheets of poly(LVal) chains.

K C Chou, H A Scheraga
PMCID: PMC347272  PMID: 6960363

Abstract

The energies of three- and five-chain antiparallel and parallel beta-sheets were minimized. Each chain consisted of six L-valine residues with CH3CO and NHCH3 end groups; the chains were considered to be equivalent, but all dihedral angles of a given chain were allowed to vary independently during energy minimization. The minimum-energy structures had a considerable right-handed twist, as observed in globular proteins. This right-handed twist is due primarily to intrachain nonbonded interactions. Such interactions between the C gamma 1H3 group of the ith residue and the C gamma 2H3 group of the (i + 2)th residue of the same chain favor a twist of either handedness over the flat structure. However, many small intrastrand pair-wise interatomic interactions involving the C gamma 1H3 and C gamma 2H3 groups, especially the interactions of these groups with the O and amide H atoms of the neighboring peptide groups, make the right-handed twisted structure energetically more favorable than the left-handed one. The intrastrand side-chain torsional energy plays a small additional role in favoring the right-twisted structure over both the flat and the left-twisted structures. The interstrand interactions favor flat structures, but they are not strong enough to overcome the intrastrand interactions that favor the twisted structure; they only decrease somewhat the extent of the right-handed twist of the beta-sheets.

Full text

PDF
7048

Selected References

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

  1. Balcerski J. S., Pysh E. S., Bonora G. M., Toniolo C. Vacuum ultraviolet circular dichroism of beta-forming alkyl oligopeptides. J Am Chem Soc. 1976 Jun 9;98(12):3470–3473. doi: 10.1021/ja00428a013. [DOI] [PubMed] [Google Scholar]
  2. Chothia C. Conformation of twisted beta-pleated sheets in proteins. J Mol Biol. 1973 Apr 5;75(2):295–302. doi: 10.1016/0022-2836(73)90022-3. [DOI] [PubMed] [Google Scholar]
  3. Lifson S., Sander C. Antiparallel and parallel beta-strands differ in amino acid residue preferences. Nature. 1979 Nov 1;282(5734):109–111. doi: 10.1038/282109a0. [DOI] [PubMed] [Google Scholar]
  4. Lotz B., Gonthier-Vassal A., Brack A., Magoshi J. Twisted single crystals of Bombyx mori silk fibroin and related model polypeptides with beta structure. A correlation with the twist of the beta sheets in globular proteins. J Mol Biol. 1982 Apr 5;156(2):345–357. doi: 10.1016/0022-2836(82)90333-3. [DOI] [PubMed] [Google Scholar]
  5. Némethy G., Scheraga H. A. Protein folding. Q Rev Biophys. 1977 Aug;10(3):239–252. doi: 10.1017/s0033583500002936. [DOI] [PubMed] [Google Scholar]
  6. Ooi T., Scott R. A., Vanderkooi G., Scheraga H. A. Conformation of analysis of macromolecules. IV. Helical structures of poly-L-alanine, poly-L-valine, poly-beta-methyl-L-aspartate, poly-gamma-methyl-L-glutamate, and poly-L-tyrosine. J Chem Phys. 1967 Jun 1;46(11):4410–4426. doi: 10.1063/1.1840561. [DOI] [PubMed] [Google Scholar]
  7. Pauling L., Corey R. B. Two Rippled-Sheet Configurations of Polypeptide Chains, and a Note about the Pleated Sheets. Proc Natl Acad Sci U S A. 1953 Apr;39(4):253–256. doi: 10.1073/pnas.39.4.253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Raghavendra K., Sasisekharan V. Conformational analysis of the right-hand twisted antiparallel beta-structure. Int J Pept Protein Res. 1979 Oct;14(4):326–338. doi: 10.1111/j.1399-3011.1979.tb01940.x. [DOI] [PubMed] [Google Scholar]
  9. Richardson J. S. The anatomy and taxonomy of protein structure. Adv Protein Chem. 1981;34:167–339. doi: 10.1016/s0065-3233(08)60520-3. [DOI] [PubMed] [Google Scholar]
  10. Salemme F. R. Conformational and geometrical properties of beta-sheets in proteins. III. Isotropically stressed configurations. J Mol Biol. 1981 Feb 15;146(1):143–156. doi: 10.1016/0022-2836(81)90370-3. [DOI] [PubMed] [Google Scholar]
  11. Salemme F. R., Weatherford D. W. Conformational and geometrical properties of beta-sheets in proteins. I. Parallel beta-sheets. J Mol Biol. 1981 Feb 15;146(1):101–117. doi: 10.1016/0022-2836(81)90368-5. [DOI] [PubMed] [Google Scholar]
  12. Salemme F. R., Weatherford D. W. Conformational and geometrical properties of beta-sheets in proteins. II. Antiparallel and mixed beta-sheets. J Mol Biol. 1981 Feb 15;146(1):119–141. doi: 10.1016/0022-2836(81)90369-7. [DOI] [PubMed] [Google Scholar]
  13. Toniolo C., Palumbo M. Solid-state infrared absorption spectra and chain arrangement in some synthetic homooligopeptides in the intermolecularly hydrogen-bonded pleated-sheet beta-conformation. Biopolymers. 1977 Jan;16(1):219–224. doi: 10.1002/bip.1977.360160116. [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