@article{oai:ir.soken.ac.jp:00004299,
 author = {桑島, 邦博 and ARAI, Munehito and KUWAJIMA, Kunihiro},
 journal = {Advances in Protein Chemistry, Advances in Protein Chemistry},
 month = {},
 note = {Publisher Summary

This chapter deals with the structure of the molten globules of various globular proteins revealed by the recent experimental studies. Recent advances in experimental techniques, including hydrogen-exchange NMR, solution X-ray scattering, and protein engineering, have provided detailed pictures of the molten globules for these proteins. The molten globule state has heterogeneous structures, in which one portion of a molecule is more organized and native-like with the other portions being less organized, although the overall structure satisfies the criteria of the molten globule state (compactness, the presence of secondary structure, and the lack of rigid tertiary structure). The chapter describes how the molten globule state has been identified as the intermediate of kinetic refolding and discusses the kinetic roles of the molten globule state in protein folding. The chapter also discusses thermodynamic stability and cooperativity of the molten globule state from the viewpoint of the hierarchy of protein folding, in which the molten globule state plays a role as a junction of two levels of the hierarchy.

We dedicate this review to the late Prof. Dr. Oleg Borisovich Ptitsyn, who passed away during our preparation of this article.},
 pages = {209--282},
 title = {Role of the molten globule state in protein folding},
 volume = {53},
 year = {2000}
}