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?-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.


ABSTRACT: The (13)C chemical shifts measured for designed ?-hairpins indicate that the structuring shifts (upfield for C? and C', downfield for C?) previously reported as diagnostic for ?-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 ?-strands. This feature of hairpins is also likely to be present in proteins. The study provides reference values for the expectation shifts for (13)C sites in ?-structures that should prove useful in the characterization of the folding equilibria of ?-sheet models.

SUBMITTER: Shu I 

PROVIDER: S-EPMC3146544 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.

Shu Irene I   Stewart James M JM   Scian Michele M   Kier Brandon L BL   Andersen Niels H NH  

Journal of the American Chemical Society 20110107 5


The (13)C 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  ...[more]

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