FEBS Letters | |
Reversal of peptide backbone direction may result in the mirroring of protein structure | |
Guptasarma, P.1  | |
[1]Centre for Cellular and Molecular Biology, Hyderabad-500 007, AP, India | |
关键词: Retroprotein; Peptide backbone direction; Sequence analysis; Structure modelling; Chirality; Protein engineering; | |
DOI : 10.1016/0014-5793(92)81333-H | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
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).
【 授权许可】
Unknown
【 预 览 】
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