Investigation of the backbone dynamics of the igg-binding domain of streptococcal protein g by heteronuclear two-dimensional 1 H-15 N nuclear magnetic resonance spectroscopy
Author:
Funder
National Institutes of Health
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560030103/fullpdf
Reference28 articles.
1. 1.67-Å X-ray structure of the B2 immunoglobulinbinding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain;Achari;Biochemistry,1992
2. Influence of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms upon longitudinal relaxation rates of 15N in macromolecules;Boyd;Chem Phys Lett,1990
3. Ribbon models of macromolecules;Carson;J Mol Graphics,1987
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