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Stabilization of \gamma-Turn Conformations in Peptides by Disulfide Bridging

Kishore, R and Balaram, P (1985) Stabilization of \gamma-Turn Conformations in Peptides by Disulfide Bridging. In: Biopolymers, 24 (11). pp. 2041-2043.


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The ideal \gamma-turn conformation in peptides is stabilized by the formation of two intramolecular hydrogen bonds. These are between the NH of residue i and the C = O of residue i + 2 (1 \rightarrow 3, $C_{11}$) and the C = O of residue i and the NH of residue i + 2 (3 \rightarrow 1, $C_7$). While this reverse-turn structural feature has been observed in proteins, unambiguous characterization of this conformation has yet to be realized in small peptides. Several examples of a single 3 \rightarrow 1 $(C_7)$ hydrogen bond have been reported in crystal structures of cyclic peptides and inferred from spectroscopic studies in apolar solvents. We wish to describe the spectroscopic characterization of a \gamma-turn conformation in a protected tripeptide, stabilized by formation of a disulfide crosslink.

Item Type: Journal Article
Publication: Biopolymers
Publisher: John Wiley & Sons, Inc
Additional Information: Copyright for this article belongs to John Wiley & Sons, Inc.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 04 Mar 2005
Last Modified: 19 Sep 2010 04:18
URI: http://eprints.iisc.ac.in/id/eprint/2869

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