Long-range order in the src SH3 folding transition state
نویسندگان
چکیده
منابع مشابه
Long-range order in the src SH3 folding transition state.
One of the outstanding questions in protein folding concerns the degree of heterogeneity in the folding transition state ensemble: does a protein fold via a large multitude of diverse "pathways," or are the elements of native structure assembled in a well defined order? Herein, we build on previous point mutagenesis studies of the src SH3 by directly investigating the association of structural ...
متن کاملCircularization changes the folding transition state of the src SH3 domain.
Native state topology has been implicated as a major determinant of protein-folding mechanisms. Here, we test experimentally the robustness of the src SH3-domain folding transition state to changes in topology by covalently constraining regions of the protein with disulfide crosslinks and then performing kinetic analysis on point mutations in the context of these modified proteins. Circularizat...
متن کاملFolding dynamics of the src SH3 domain.
The thermodynamics and kinetics of folding of the chicken src SH3 domain were characterized using equilibrium and stopped-flow fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) hydrogen exchange experiments. As found for other SH3 domains, guanidinium chloride (GdmCl) denaturation melts followed by both fluorescence and circular dichroism were nearly superimposable, in...
متن کاملAn R-Helical Burst in the src SH3 Folding Pathway
Src SH3 is a small all-â-sheet protein composed of a single domain. We studied the folding behavior of src SH3 at various conditions by circular dichroism (CD), fluorescence, and X-ray solution scattering methods. On the src SH3 folding pathway, an R-helix-rich intermediate appeared not only at subzero temperatures but also above 0 °C. The fraction of R-helix in the kinetically observed interme...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2000
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.97.13.7084