Analysis of the steric strain in the polypeptide backbone of protein molecules
Proteins Structure Function and Bioinformatics1991Vol. 11(3), pp. 223–229
Citations Over TimeTop 10% of 1991 papers
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.
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