REVERSALS OF POLYPEPTIDE CHAIN IN GLOBULAR PROTEINS

A. S. KOLASKAR, V. RAMABRAHMAM, K. V. SOMAN

    Research output: Contribution to journalArticle

    38 Scopus citations

    Abstract

    A simple algorithm has been developed to detect β‐bends and ‘loops’‐chain reversals containing five amino acid residues, using only coordinates of Cα‐atoms from crystal structure data of globular proteins using the above algorithm. Analysis of bends have showed that the total number of bends in each protein (TB) is linearly related to total number of non‐hydrophobic residues in that protein which in turn is related linearly to total number of amino acid residues. Secondly, we found that a large number of consecutive bends occur in each protein which give rise to on an average only three 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.

    Original languageEnglish (US)
    Pages (from-to)1-11
    Number of pages11
    JournalInternational Journal of Peptide and Protein Research
    Volume16
    Issue number1
    DOIs
    StatePublished - Jul 1980

    Keywords

    • polypeptide chain reversals
    • protein data analysis
    • β‐bends and “loops”

    ASJC Scopus subject areas

    • Biochemistry

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