nuclear magnetic resonance;
NMR;
protein structure;
protein dynamics;
protein thermodynamics;
Src homology 2 domain;
SH2;
D O I:
10.1139/o97-023
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
An understanding of the role played by a protein in cellular function requires a detailed picture of its three-dimensional structure as well as an appreciation of how the structure varies as a function of time as a result of molecular dynamics. Over the past several years, multidimensional, multinuclear solution NMR spectroscopy has become a powerful technology for obtaining both structural and dynamical information on proteins and protein-ligand systems. In the present review, a number of new methodological advances are highlighted that have significantly improved the quality of NMR spectra of biomolecules and have increased the molecular weight limitations previously imposed on NMR-based structural studies of macromolecules. Applications of this technology to a number of protein systems currently studied in my laboratory are presented.