| Literature DB >> 12139938 |
Munehito Arai1, Kazuki Ito, Tomonao Inobe, Masaharu Nakao, Kosuke Maki, Kiyoto Kamagata, Hiroshi Kihara, Yoshiyuki Amemiya, Kunihiro Kuwajima.
Abstract
To monitor the fast compaction process during protein folding, we have used a stopped-flow small-angle X-ray scattering technique combined with a two-dimensional charge-coupled device-based X-ray detector that makes it possible to improve the signal-to-noise ratio of data dramatically, and measured the kinetic refolding reaction of alpha-lactalbumin. The results clearly show that the radius of gyration and the overall shape of the kinetic folding intermediate of alpha-lactalbumin are the same as those of the molten globule state observed at equilibrium. Thus, the identity between the kinetic folding intermediate and the equilibrium molten globule state is firmly established. The present results also suggest that the folding intermediate is more hydrated than the native state and that the hydrated water molecules are dehydrated when specific side-chain packing is formed during the change from the molten globule to the native state.Entities:
Mesh：
Substances：
Year: 2002 PMID： 12139938 DOI： 10.1016/s0022-2836(02)00566-1
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469