ArticleProtein science : a publication of the Protein Society2001
A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Proline Peptide Bond Isomerization in Ubiquitin Under Folding and Denaturing Conditions by Pressure-Jump NMR.Journal of molecular biology · 2024Article
- pH (low) insertion peptide (pHLIP) inserts across a lipid bilayer as a helix and exits by a different path.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.Protein science : a publication of the Protein Society · 2009Article
- 3S-fluoroproline as a probe to monitor proline isomerization during protein folding by 19F-NMR.Chemical communications (Cambridge, England) · 2009Article
- Protein folding: then and now.Archives of biochemistry and biophysics · 2008Article
- Folding and unfolding of a non-fluorescent mutant of green fluorescent protein.Journal of physics. Condensed matter : an Institute of Physics journal · 2007Article
- Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK.Protein science : a publication of the Protein Society · 2006Article
- Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe.Comparative and functional genomics · 2005Article
- Apo-azurin folds via an intermediate that resembles the molten-globule.Protein science : a publication of the Protein Society · 2004Article
- Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.Protein science : a publication of the Protein Society · 2004Article
- In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.Protein science : a publication of the Protein Society · 2003Article
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6 authors.
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Abstract
The folding of apo-pseudoazurin, a 123-residue, predominantly beta-sheet protein with a complex Greek key topology, has been investigated using several biophysical techniques. Kinetic analysis of refolding using far- and near-ultraviolet circular dichroism (UV CD) shows that the protein folds slowly to the native state with rate constants of 0.04 and 0.03 min(-1), respectively, at pH 7.0 and at 15 degrees C. This process has an activation enthalpy of approximately 90 kJ/mole and is catalyzed by cyclophilin A, indicating that folding is limited by trans-cis proline isomerization, presumably around the Xaa-Pro 20 bond that is in the cis isomer in the native state. Before proline isomerization, an intermediate accumulates during folding. This species has a substantial signal in the far-UV CD, a nonnative signal in the near-UV CD, exposed hydrophobic surfaces (judged by 1-anilino naphthalenesulphonate binding), a noncooperative denaturation transition, and a dynamic structure (revealed by line broadening on the nuclear magnetic resonance time scale). We compare the properties of this intermediate with partially folded states of other proteins and discuss its role in folding of this complex Greek key protein.
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