ArticleBiophysical journal2004
Multiple folding pathways of the SH3 domain.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- Conserved patterns and interactions in the unfolding transition state across SH3 domain structural homologues.Protein science : a publication of the Protein Society · 2021Article
- The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulations.BMC structural biology · 2011Article
- Toward a molecular theory of early and late events in monomer to amyloid fibril formation.Annual review of physical chemistry · 2011Review
- Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- An enhanced partial order curve comparison algorithm and its application to analyzing protein folding trajectories.BMC bioinformatics · 2008Article
- Mechanisms of protein folding.European biophysics journal : EBJ · 2008Review
- An entropic perspective of protein stability on surfaces.Biophysical journal · 2008Article
- Protein folding: then and now.Archives of biochemistry and biophysics · 2008Article
- Multiscale modeling of nucleosome dynamics.Biophysical journal · 2007Article
- Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Chemical reviews · 2006Review
- Confinement effects on the thermodynamics of protein folding: Monte Carlo simulations.Biophysical journal · 2006Article
- Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 undergoes a rapid folding transition with minimal kinetic barriers-and observe that below this temperature the model protein may undergo a folding transition by multiple folding pathways via only one or two intermediates. Our findings suggest the hypothesis that the SH3 domain, a protein fold for which only two-state folding kinetics was observed in previous experiments, may exhibit intermediate states under conditions that strongly stabilize the native state.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.