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One-bond and two-bond J couplings help annotate protein secondary-structure motifs: J-coupling indexing applied to human endoplasmic reticulum protein ERp18

Schmidt, Jürgen M., Zhou, Shen, Rowe, Michelle L., Howard, Mark J., Williamson, Richard A., Löhr, Frank (2011) One-bond and two-bond J couplings help annotate protein secondary-structure motifs: J-coupling indexing applied to human endoplasmic reticulum protein ERp18. Proteins: Structure, Function, and Bioinformatics, 79 (2). pp. 428-443. ISSN 0887-3585. (doi:10.1002/prot.22893) (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:26247)

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. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1002/prot.22893

Abstract

NMR coupling constants, both direct one-bond (1J) and geminal two-bond (2J), are employed to analyze the protein secondary structure of human oxidized ERp18. Coupling constants collected and evaluated for the 18-kDa protein comprise 1268 values of 1JCaHa, 1JCaCb, 1JCaC', 1JC'N', 1JN'Ca, 1JN'HN, 2JCaN', 2JHNCa, 2JC'HN, and 2JHaC'. Comparison with 1J and 2J data from reference proteins and pattern analysis on a per-residue basis permitted main-chain f,y torsion-angle combinations of many of the 149 amino-acid residues in ERp18 to be narrowed to particular secondary-structure motifs. J-coupling indexing is here being developed on statistical criteria and used to devise a ternary grid for interpreting patterns of relative values of J. To account for the influence of the varying substituent pattern in different amino-acid sidechains, a table of residue-type specific threshold values was compiled for discriminating small, medium and large categories of J. For the 15-residue insertion that distinguishes the ERp18 fold from that of thioredoxin, the J-coupling data hint at a succession of five isolated type-I b turns at progressively shorter sequence intervals, in agreement with the crystal structure.

Item Type: Article
DOI/Identification number: 10.1002/prot.22893
Subjects: Q Science
Q Science > QD Chemistry
Q Science > QC Physics
Divisions: Faculties > Sciences > School of Biosciences
Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: Jurgen M Schmidt
Date Deposited: 19 Jan 2011 15:17 UTC
Last Modified: 28 May 2019 15:55 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/26247 (The current URI for this page, for reference purposes)
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