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Variation in protein C -alpha-related one-bond J couplings

Schmidt, Jürgen M., Howard, Mark J., Maestre-Martinez, Mitcheell, Perez, Carlos S, Löhr, Frank (2009) Variation in protein C -alpha-related one-bond J couplings. Magnetic Resonance in Chemistry, 47 (1). pp. 16-30. ISSN 0749-1581. (doi:10.1002/mrc.2337) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:22666)

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Four types of polypeptide (1)J(C alpha X) couplings are examined, involving the main-chain carbon C(alpha) and either of four possible substituents. A total 3105 values of (1)J(C alpha H alpha), (1)J(C alpha C beta), (1)J(C alpha C'), and (1)J(C alpha N') were collected from six proteins, averaging 143.4 +/- 3.3, 34.9 +/- 2.5, 52.6 +/- 0.9, and 10.7 +/- 1.2 Hz, respectively. Analysis of variances (ANOVA) reveals a variety of factors impacting on (1)J and ranks their relative statistical significance and importance to biomolecular NMR structure refinement. Accordingly, the spread in the (1)J values is attributed, in equal proportions, to amino-acid specific substituent patterns and to polypeptide-chain geometry, specifically torsions phi, psi, and chi(1) circumjacent to C(alpha). The (1)J coupling constants correlate with protein secondary structure. For alpha-helical phi, psi combinations, (1)J(C alpha H alpha) is elevated by more than one standard deviation (147.8 Hz), while both (1)J(C alpha N') and (1)J(C alpha C beta) fall short of their grand means (9.5 and 33.7 Hz). Rare positive phi torsion angles in proteins exhibit concomitant small (1)J(C alpha H alpha) and (1)J(C alpha N') (138.4 and 9.6 Hz) and large (1)J(C alpha C beta) (39.9 Hz) values. The (1)J(C alpha N') coupling varies monotonously over the phi torsion range typical of beta-sheet secondary structure and is largest (13.3 Hz) for phi around -160 degrees. All four coupling types depend on psi and thus help determine a torsion that is notoriously difficult to assess by traditional approaches using (3)J. Influences on (1)J stemming from protein secondary structure and other factors, such as amino-acid composition, are largely independent.

Item Type: Article
DOI/Identification number: 10.1002/mrc.2337
Additional information: 1097-458X (Electronic) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Nuclear Magnetic Resonance, Biomolecular/*methods Protein Structure, Secondary Proteins/*chemistry
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Funders: Biotechnology and Biological Sciences Research Council (
European Commission (
Depositing User: M.J. Howard
Date Deposited: 15 Sep 2009 09:36 UTC
Last Modified: 12 Jul 2022 10:39 UTC
Resource URI: (The current URI for this page, for reference purposes)

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Schmidt, Jürgen M..

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Howard, Mark J..

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