Fast events in protein folding

Understanding how proteins fold is one of the central problems in biochemistry. A new generation of kinetic experiments has emerged to investigate the mechanisms of protein folding on the previously inaccessible submillisecond time scale. These experiments provide the first glimpse of processes such...

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Bibliographic Details
Published in:Structure 1996-10, Vol.4 (10), p.1133-1139
Main Authors: Eaton, William A, Thompson, Peggy A, Chan, Chi-Kin, Hage, Stephen J, Hofrichter, James
Format: Article
Language:English
Subjects:
Apoproteins - chemistry
Cytochrome c Group - chemistry
Kinetics
Models, Molecular
Myoglobin - chemistry
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Thermodynamics
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Summary:Understanding how proteins fold is one of the central problems in biochemistry. A new generation of kinetic experiments has emerged to investigate the mechanisms of protein folding on the previously inaccessible submillisecond time scale. These experiments provide the first glimpse of processes such as secondary structure formation, local hydrophobic collapse, global collapse to compact denatured states, and fast barrier crossings to the native state. Key results are summarized and discussed in terms of the statistical energy landscape theory of protein folding.
ISSN:0969-2126
1878-4186
DOI:10.1016/S0969-2126(96)00121-9