作者
Hans Rudolf Bosshard, Eberhard Dürr, Thomas Hitz, Ilian Jelesarov
发表日期
2001/3/27
期刊
Biochemistry
卷号
40
期号
12
页码范围
3544-3552
出版商
American Chemical Society
简介
Coiled coils are simple models for studying the association of two polypeptide chains to form a folded protein. Previous work has shown that the folding of a coiled coil can be described by a two-state transition between two unfolded monomeric peptide chains and a folded coiled coil dimer. Here we report the thermodynamic activation parameters for the folding and unfolding of two unrelated coiled coils: C62GCN4 and A2. C62GCN4 corresponds to the 62 C-terminal residues of yeast transcription factor GCN4. The peptide forms a dimeric coiled coil through its 33 C-terminal residues. A2 is a designed 30-residue dimeric coiled coil whose folding is induced by low pH [Dürr, E., Jelesarov, I., and Bosshard, H. R. (1999) Biochemistry 38, 870−880]. Folding and unfolding were assessed under identical native buffer conditions so that the microscopic reversibility applied and the transition state was the same for folding …
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HR Bosshard, E Dürr, T Hitz, I Jelesarov - Biochemistry, 2001