Transient Helical Structure during PI3K and Fyn SH3 Domain Folding
نویسندگان
چکیده
منابع مشابه
Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment.
A complete description of how a protein folds requires the characterization of intermediate conformations traversed during the folding transition. We have calculated dynamics trajectories of a simplified model of the Fyn SH3 domain with a native-centric potential energy function. Analysis of the resulting site-resolved energy trajectory identifies an ensemble of intermediate conformations for f...
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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...
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Experimental observations suggest that proteins follow different folding pathways under different environmental conditions. We perform molecular dynamics simulations of a model of the c-Crk SH3 domain over a broad range of temperatures, and identify distinct pathways in the folding transition. We determine the kinetic partition temperature-the temperature for which the c-Crk SH3 domain undergoe...
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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: The Journal of Physical Chemistry B
سال: 2013
ISSN: 1520-6106,1520-5207
DOI: 10.1021/jp400167s