Characterization of folding the four-helix bundle protein Rop by real-time NMR.
Characterization of folding the four-helix bundle protein Rop by real-time NMR.
复制标题
通过实时 NMR 表征折叠四螺旋束蛋白 Rop。
DOI：
10.1093/protein/gzm081
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Regan,Lynne
中科院分区：
文献类型：
--
作者：
vanNuland,NicoAJ;Dobson,ChristopherM;Regan,Lynne
Rop is a four-helix bundle protein composed of two identical helix-loop-helix monomers. Protein folding monitored by stopped-flow fluorescence or CD exhibits biphasic kinetics when folding to low final denaturant concentrations. As the final concentration of denaturant is increased, the amplitude of the fast phase decreases, until at the highest concentrations the kinetics appear monophasic. We propose that the fast phase represents the formation of an intermediate. Here, we use real-time NMR to detect the formation of this intermediate and to characterize its structural features.
