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Communication

β-Sheet ¹³C Structuring Shifts Appear Only at the H-Bonded Sites of Hairpins

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Irene Shu, James M. Stewart, Michele Scian, Brandon L. Kier, and Niels H. Andersen*

Department of Chemistry, University of Washington, Seattle, Washington 98195, United States

J. Am. Chem. Soc., 2011, 133 (5), pp 1196–1199

DOI: 10.1021/ja1088953

Publication Date (Web): January 7, 2011

andersen@chem.washington.edu

Section:

General Biochemistry

Abstract

The ¹³C chemical shifts measured for designed β-hairpins indicate that the structuring shifts (upfield for Cα and C′, downfield for Cβ) previously reported as diagnostic for β-structuring in proteins appear only at the H-bonded strand residues. The resulting periodicity of structuring shift magnitudes is not, however, a consequence of H-bonding status; rather, it reflects a previously unrecognized alternation in the backbone torsion angles of β-strands. This feature of hairpins is also likely to be present in proteins. The study provides reference values for the expectation shifts for ¹³C sites in β-structures that should prove useful in the characterization of the folding equilibria of β-sheet models.

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History

Published In Issue February 09, 2011
Article ASAPJanuary 07, 2011
Received: October 01, 2010

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Communication

β-Sheet ¹³C Structuring Shifts Appear Only at the H-Bonded Sites of Hairpins