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Reversal of peptide backbone direction may result in the mirroring of protein structure
Author(s) -
Guptasarma P.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81333-h
Subject(s) - mirroring , side chain , chain (unit) , peptide , chirality (physics) , mirror image , stereochemistry , protein structure , crystallography , chemistry , topology (electrical circuits) , sequence (biology) , physics , chiral symmetry , mathematics , combinatorics , biochemistry , optics , communication , astronomy , sociology , nambu–jona lasinio model , quark , polymer , organic chemistry , quantum mechanics
In linear polypeptides, inversion of amino acid chirality (all‐ l to all‐ d ) achieves a mirroring of side chain positions and interactions in conformational space. A similar mirroring of side chain positions is independently achieved by a reversal of the direction of the peptide backbone (retro modification). Thus, while an all‐ d chain could be expected to adopt a perfect ‘mirror image’ of the three‐dimensional structure of its parent all‐ l protein, the retro‐all‐ l chain could be expected to adopt a topological equivalent of such a mirror image, through the symmetry transformations of side chain interactions. These notions, supported by sequence analyses, modelling studies, and evidence relating to the activity of ‘retro‐inverso’ peptides, are extended towards the proposal, that the backbone reversed chain of a large globular protein might recognize the chiral opposite of the parent protein's substrate(s).