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Energetics of protein structure and folding
Author(s) -
Goldenberg David P.,
Creighton Thomas E.
Publication year - 1985
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360240114
Subject(s) - chemistry , energetics , protein folding , limiting , folding (dsp implementation) , lattice protein , phi value analysis , isomerization , kinetics , downhill folding , crystallography , energy landscape , biophysics , chemical physics , thermodynamics , biochemistry , mechanical engineering , physics , electrical engineering , quantum mechanics , engineering , catalysis , biology
The available experimental date 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 high‐energy 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.