Microsecond Rearrangements of Hydrophobic Clusters in an Initially Collapsed Globule Prime Structure Formation during the Folding of a Small Protein
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- 作者：Rama Reddy Goluguri ; Jayant B. Udgaonkar ; jayant@ncbs.res.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：MG ; molten globule ; N state ; native state ; U ; unfolded state ; UC ; collapsed U state ; MNEI ; monellin ; SAXS ; small angle X-ray scattering ; GdnHCl ; guanidine hydrochloride ; FRET ; fluorescence resonance energy transfer ; IAEDANS ; 5-((((2-iodoacetyl) amino)-ethyl)amino)-naphthalene-1-sulfonic acid ; ANS ; 1-anilino napthalene8-sulfonate ; TNB ; thionitrobenzoate ; NATA ; N-acetyl-L-tryptophanamide ; IVE ; intermediate ; MEC ; minimum energy compact ; ESI-MS ; electrospray ionization mass spectrometry
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3102-3117
- 全文大小：1970 K
文摘
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The nature and role of sub-millisecond events during protein folding are poorly understood.
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Sub-millisecond folding events of monellin were studied using multiple probes.
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Native and nonnative structures assemble and disassemble noncooperatively during sub-millisecond folding.
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Two sequential chain rearrangements of hydrophobic clusters prime structure formation at 1 ms of folding.