Using potential energy formulas for variation of bond angles and for w-distortion, the conformation of minimum energy for the cis form of the petide unit has been worked out. This agrees very well with the corresponding set of atoms in the crystal structure of Leu-Pro-Gly and the dimensions of a sta
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
β Scribed by C. M. Venkatachalam
- Book ID
- 102761333
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1968
- Tongue
- English
- Weight
- 572 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The general conformations of a system of three linked peptide units are studied, and it is found that there are three types of conformations which contain NH. . .O hydrogen bonding between the first and the third units. One of them is part of a 3lrhelix, while the other two are noiihelical. The two iionhelical conformations are very similar, and in both the cases the peptide chain turns around, reversing the direction of progress. Such a conformation can therefore occur in the region where a polypeptide chain folds back on itself, as in the cross-p structure. The method of representing these interesting tripeptide conformations in a (+,+) map is described. Examples of such hydrogen-bonded, nonhelical conformations which occur in peptides and proteins are discussed-e.g., in cyclohexaglycyl, an open tetrapeptide Gly-L-Pro-L-Leu-Gly, and in parts of the lysozyme chain.
π SIMILAR VOLUMES
Knowledge of chemical shift-structure relationships could greatly facilitate the NMR chemical shift assignment and structure refinement processes that occur during peptide/protein structure determination via NMR spectroscopy. To determine whether such correlations exist for polar side chain containi