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Stable conformations of dipeptides

Stable conformations of dipeptides Stable Conformations of Dipeptides The conformational properties of small peptides have been studied extensively by both experimentall-7 and theoretical8-lO techniques. A detailed understanding of these systems is important for the investigation of the folding of polypeptides and proteins since they should indicate the role of short-range interactions in stabilizing these larger structures. Although many techniques have been used, perhaps the most definitive results for the solution conformations of compounds consisting of a single side chain and two peptide bonds (I), referred to as dipeptides, have come from infrared and nuclear magnetic resonance spe~troscopy.'.~*4 Scheme I Several of these studies have endeavored to interpret the relative amounts of the several conformations of the dipeptide by combining the spectroscopic data with theoretical calculations.3J These reports have indicated that there are essentially two conformations (C, and C,, with dihedral angles +,$ = -170°,1700 and -80°,800, respectivelyll) present in dilute carbon tetrachloride solution and that both of these contain intramolecular hydrogen bonds. However, it is possible to interpret the available experimental evidence on the basis that there are a t least three conformations of dipeptides in CClr solutions whenever R is larger than a hydrogen atom. 'This reevaluation of the spectroscopic results http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Stable conformations of dipeptides

Biopolymers , Volume 12 (9) – Sep 1, 1973

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References (19)

Publisher
Wiley
Copyright
Copyright © 1973 John Wiley & Sons, Inc.
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/bip.1973.360120920
pmid
4744757
Publisher site
See Article on Publisher Site

Abstract

Stable Conformations of Dipeptides The conformational properties of small peptides have been studied extensively by both experimentall-7 and theoretical8-lO techniques. A detailed understanding of these systems is important for the investigation of the folding of polypeptides and proteins since they should indicate the role of short-range interactions in stabilizing these larger structures. Although many techniques have been used, perhaps the most definitive results for the solution conformations of compounds consisting of a single side chain and two peptide bonds (I), referred to as dipeptides, have come from infrared and nuclear magnetic resonance spe~troscopy.'.~*4 Scheme I Several of these studies have endeavored to interpret the relative amounts of the several conformations of the dipeptide by combining the spectroscopic data with theoretical calculations.3J These reports have indicated that there are essentially two conformations (C, and C,, with dihedral angles +,$ = -170°,1700 and -80°,800, respectivelyll) present in dilute carbon tetrachloride solution and that both of these contain intramolecular hydrogen bonds. However, it is possible to interpret the available experimental evidence on the basis that there are a t least three conformations of dipeptides in CClr solutions whenever R is larger than a hydrogen atom. 'This reevaluation of the spectroscopic results

Journal

BiopolymersWiley

Published: Sep 1, 1973

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