Relationships between the Precision of High-Resolution Protein NMR Structures, Solution-Order Parameters, and Crystallographic B Factors

Authors

Robert Powers, University of Nebraska - LincolnFollow
G. Marius Clore, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Daniel S. Garrett, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Angela M. Gronenborn, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health

Date of this Version

1993

Citation

Journal of Magnetic Resonance, Series B 101, 325-327 (1993)

Comments

U.S. Government Work

Abstract

One of the principal motivations for studying proteins by nuclear magnetic resonance stems from the desire to describe the solution structure of these molecules as compared to the generally perceived static picture obtained by X-ray crystallography. Indeed, it is one of the unique features of NMR spectroscopy that in addition to structural data, dynamic properties can be probed and characterized by measuring relaxation parameters. Furthermore, any mobility of the protein in solution will necessarily modulate the measured NMR parameters and should influence the resulting structure. It has been argued that regions of a protein that are highly mobile would be expected to be defined to a lesser degree of precision than regions that are rigid (1. 2 ).