重水素交換ＮＭＲ分光法によるタンパク質立体構造の揺らぎの研究

Abstract

The NMR structure determination method is well established as a powerful tool in protein research, but an amide hydrogen-exchange NMR is also a unique approach, providing important information on structural fluctua-tions in protein at the resolution of an individual residue. Here we survey hydrogen-deuterium (H-D) exchange NMR studies on protein dynamics and folding. The purpose of this article is to explain what the H-D exchange NMR method is, and to demonstrate how to obtain information about protein dynamics from such experiments. H-D exchange NMR experiments for lysozyme variants lacking some of the disulfide bridges are reviewed as an ex-ample of studies. In addition, recent developments in H-D exchange NMR methods are surveyed with concern about pulsed hydrogen-exchange labeling to detect kinetic folding intermediates. Finally, we describe our challenge to study structurally blocked hydrogens in lysozyme variants in the non-native state by using the H-D exchange NMR method.