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Analysis of the steric strain in the polypeptide backbone of protein molecules

✍ Scribed by Dr. Osnat Herzberg; John Moult

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
623 KB
Volume
11
Category
Article
ISSN
0887-3585

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✦ Synopsis

Abstract

The extent to which local strain is present in the polypeptide backbone of folded protein molecules has been examined. The occurrence of steric strain associated with nonproline cis peptide bonds and energetically unfavorable main chain dihedral angles can be identified reliably from the well ordered parts of high resolution, refined crystal structures. The analysis reveals that there are relatively few sterically strained features. Those that do occur are located overwhelmingly in regions concerned with function. We attribute this to the greater precision necessary for ligand binding and catalysis, compared with the requirements of satisfactory folding.

πŸ“œ SIMILAR VOLUMES

An analysis of the amide I mode in the v
An analysis of the amide I mode in the vibrational spectra of unordered polypeptides and proteins
✍ P. C. Painter; M. M. Coleman πŸ“‚ Article πŸ“… 1978 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 610 KB

## Abstract The difference in the observed frequency of the amide I mode between the Raman and ir spectra of many unordered polypeptides is interpreted in terms of a model in which sequences of amide groups have similar Ο•, ψ angles. The splittings due to intramolecular interactions for the infinite