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Calcium-binding proteins afford calibration of dihedral-angle dependence of 3J(NC(gamma)) coupling constant in aspartate and asparagine residues.

作者信息

Juranić Nenad, Atanasova Elena, Moncrieffe Martin C, Prendergast Franklyn G, Macura Slobodan

机构信息

Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, MN 55905, USA.

出版信息

J Magn Reson. 2005 Aug;175(2):222-5. doi: 10.1016/j.jmr.2005.04.008.

DOI:10.1016/j.jmr.2005.04.008
PMID:15907387
Abstract

Calibration of the 3J(NC(gamma)) couplings across the N-C(alpha)-C(beta)-C(gamma) fragment of aspartate and asparagine residues is afforded by two interactions that produce fixed conformations of the side chains in solution. One is the binding of these side chains to calcium ions; the other is the H-bond interaction of these side chains with a backbone amide.

摘要

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