作者
Jill A Zitzewitz, Osman Bilsel, Jiabin Luo, Bryan E Jones, C Robert Matthews
发表日期
1995/10/1
期刊
Biochemistry
卷号
34
期号
39
页码范围
12812-12819
出版商
American Chemical Society
简介
Revised Manuscript Received August 17, 1995® abstract: Leucine zipper peptides provide simple model systems for studying both the intramolecular and intermolecular interactions that govern protein folding. The synthetic 33-residue peptide GCN4-pl, derived from the yeast transcriptional activator GCN4, forms a stable bimolecular coiled-coil structure [O’Shea, E. K „Klemm, J. D „Kim, P. S „& Alber, T.(1991) Science 254, 539-544], The guanidine-HC1 induced equilibrium unfolding of this peptide at 5 C and pH 7.0 yields a standard state free energy of 10.49±0.23 kcal (mol dimer)-1 when fit to a two-state model involving the nativedimer and the unfolded monomer. The unfolding and refolding kinetics of GCN4-pl were monitored by stopped-flow circular dichroism spectroscopy as a function of both peptide concentration and final denaturant concentration. The unfolding kinetics displayed single-exponential behavior …
引用总数
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JA Zitzewitz, O Bilsel, J Luo, BE Jones, CR Matthews - Biochemistry, 1995