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Energetics of protein structure and folding

✍ Scribed by David P. Goldenberg; Thomas E. Creighton

Publisher
Wiley (John Wiley & Sons)
Year
1985
Tongue
English
Weight
930 KB
Volume
24
Category
Article
ISSN
0006-3525

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✦ Synopsis

The available experimental data on the kinetics of unfolding and refolding of small proteins are reviewed. Excluding slow transitions in the unfolded protein due to cis- trans isomerization of peptide bonds, the rate-limiting transition state in both unfolding and refolding is concluded to be a highenergy distortion of the fully folded state. Partially folded intermediates are undoubtedly important for folding, but their formation is normally not rate limiting. A simple model is used to illustrate some of the aspects of protein-folding energetics.

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