This article reviews heteronuclear NMR techniques that are used to characterize the 3D structures and internal molecular dynamics of proteins in solution. Applications to several proteins that have been studied in our laboratory are presented. Topics discussed include sequential assignments, the use of nuclear Overhauser enhancement spectroscopy (NOESY) and residual dipolar coupling restraints to determine protein structure, and the use of relaxation measurements to obtain information about protein internal motions. Also discussed are recent computational approaches directed at increasing the efficiency of structure determination, as well as new methods for studying large proteins.
IUPAC Polymer Conference on the Mission and Challenges of Polymer Science and Technology (IUPAC PC2002), Kyoto, Japan, 2002-12-02–2002-12-05
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