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 beta-bends and 'loops'-chain reversals containing five 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 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
StatePublished - Jul 1980
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kolaskar, A. S., Ramabrahmam, V., & Soman, K. V. (1980). Reversals of polypeptide chain in globular proteins. International Journal of Peptide and Protein Research, 16(1), 1-11.