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Chemistry of Natural Compounds

, Volume 11, Issue 5, pp 660–665 | Cite as

Theoretical conformational analysis of tripeptides with a glycine residue

  • V. Z. Pletnev
  • F. A. Kadymova
  • E. M. Popov
Article

Summary

1. The conformational states of glycine residues — R, B, L, P — in the low-energy forms of the tripeptides (I–III) are found with equal frequency.

2. The conformations of the main chain in sections of protein with glycine residues correspond to the preferred forms of the tripeptide fragments (I–III).

3. The close-, medium-, and long-range interactions in proteins do not contradict one another and exist at the favorable forms of the main chain.

Keywords

Main Chain Optimum Form Conformational State Glycine Residue Favorable Form 

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Copyright information

© Plenum Publishing Corporation 1976

Authors and Affiliations

  • V. Z. Pletnev
  • F. A. Kadymova
  • E. M. Popov

There are no affiliations available

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