Two-dimensional nuclear magnetic resonance spectroscopy of proteins: an overview.

Publisher Summary This chapter discusses the two dimensional nuclear magnetic resonace spectroscopy of protein. NMR spectroscopy is the leading technique for obtaining structural and dynamic information at the atomic level about proteins in solution. It provides an efficient method for measuring dynamic, kinetic, and thermodynamic parameters (e.g., correlation times, order parameters, hydrogen exchange rates, and pKa values) in peptides and small proteins. NMR is the only serious competitor to single-crystal diffraction analysis for modeling three-dimensional structure of small proteins. NMR analysis is complementary to crystallography in providing a means of determining whether the protein structure is the same in solution as in the solid state. The protein NMR field appears to be entering a new phase. Available and newly emerging 2D NMR methods make it possible to resolve and assign signals from a large number of 1 H, 13 C, and 15 N nuclei in proteins of M r - 2 relaxation will prevent a dramatic increase in this limit.

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