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Peptide Bond Distortion and the Curvature of α-helices

Chakrabarti, P. and Bernard, M. and Rees, D. C. (1986) Peptide Bond Distortion and the Curvature of α-helices. Biopolymers, 25 (6). pp. 1087-1093. ISSN 0006-3525. doi:10.1002/bip.360250609.

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Solvent accessible peptide bonds in proteins exhibit a 1–3° compression of the OCN bond angle and a corresponding expansion of the NCCa bond angle, relative to buried peptide bonds. These changes are consistent with an increase in hydrogen bonding to the carbonyl oxygen accompanying solvent exposure (J. D. Dunitz and F. K. Winkler, (1975) Acta Cryst.B31, 251–263). For amphiphilic structures such as α-helices, systematic differences in peptide-bond geometry between solvent-exposed and buried residues will generate significant curvature. A decrease of 4° in the OCN bond angle between hydrophilic and hydrophobic sides of an amphiphilic helix will lead to smooth bending, with a radius of curvature of about 70 Å. This curvature is in the range observed for α-helices in proteins. Helix curvature is estimated to have only a small effect on the magnitude and direction of the helical dipole moment.

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Rees, D. C.0000-0003-4073-1185
Additional Information:© 1986 John Wiley & Sons, Inc. Received August 13, 1985; Accepted January 6, 1986. This work was supported in part by NIH grant GM31875 and an NSF Presidential Young Investigators Award.
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NSF Presidential Young Investigators AwardUNSPECIFIED
Issue or Number:6
Record Number:CaltechAUTHORS:20150210-094502630
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Official Citation:Chakrabarti, P., Bernard, M. and Rees, D. C. (1986), Peptide-bond distortions and the curvature of α-helices. Biopolymers, 25: 1087–1093. doi: 10.1002/bip.360250609
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ID Code:54637
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Deposited On:11 Feb 2015 01:01
Last Modified:10 Nov 2021 20:36

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