Shortle D R
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Curr Opin Struct Biol. 1996 Feb;6(1):24-30. doi: 10.1016/s0959-440x(96)80091-1.
Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist for detecting fractionally populated alpha helices and beta strands, but defining transient interactions among side chains is proving more problematic. The non-native states of several small proteins are being intensively investigated to address a number of questions about protein folding.
已确立的核磁共振方法越来越多地应用于蛋白质的非天然状态。对于小的变性蛋白质，质子、15N和13C共振的完全归属通常很直接。存在用于检测部分占据的α螺旋和β链的灵敏方法，但确定侧链之间的瞬时相互作用已证明更具挑战性。几种小蛋白质的非天然状态正在被深入研究，以解决一些关于蛋白质折叠的问题。
