REVERSALS OF POLYPEPTIDE CHAIN IN GLOBULAR PROTEINS
- 1 July 1980
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 16 (1) , 1-11
- https://doi.org/10.1111/j.1399-3011.1980.tb02929.x
Abstract
A simple algorithm was developed to detect .beta.-bends and loops-chain reversals containing 5 amino acid residues, using only coordinates of C.alpha.-atoms from crystal structure data of globular proteins using the above algorithm. Analysis of bends have shown that the total number of bends in each protein (TB) is linearly related to the total number of non-hydrophobic residues in that protein which, in turn, is related linearly to the total number of amino acid residues. A large number of consecutive bends occur in each protein, which give rise to, on an average, only 3 independent residues per turn. Positional preference of amino acid residues in chain reversals is stressed. Consideration of pairs of amino acid residues in positions (i + 1) and (i + 2) of bends seems to provide a more reliable basis for predicting chain reversals in proteins.Keywords
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