Cooperativity in two-state protein folding kinetics. Export

@article{citeulike:985371, abstract = {We present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For CI2, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts well the average Phi-values for secondary structures. The barrier to folding is the formation of predominantly local structures such as helices and hairpins, which are needed to bring nonlocal pairs of amino acids into contact.}, address = {Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, USA. Thomas. Weikl@mpikg-golm.mpg.de}, author = {Weikl, T. R. and Palassini, M. and Dill, K. A.}, citeulike-article-id = {985371}, citeulike-linkout-0 = {http://dx.doi.org/10.1110/ps.03403604}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/14978313}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=14978313}, doi = {10.1110/ps.03403604}, issn = {0961-8368}, journal = {Protein science : a publication of the Protein Society}, keywords = {folding, theory}, month = {March}, number = {3}, pages = {822--829}, posted-at = {2009-07-21 21:51:30}, priority = {0}, title = {Cooperativity in two-state protein folding kinetics.}, url = {http://dx.doi.org/10.1110/ps.03403604}, volume = {13}, year = {2004} }

TY - JOUR ID - citeulike:985371 L3 - citeulike-article-id:985371 N2 - We present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For CI2, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts well the average Phi-values for secondary structures. The barrier to folding is the formation of predominantly local structures such as helices and hairpins, which are needed to bring nonlocal pairs of amino acids into contact. IS - 3 JF - Protein science : a publication of the Protein Society SN - 0961-8368 AD - Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, USA. Thomas. Weikl@mpikg-golm.mpg.de EP - 829 TI - Cooperativity in two-state protein folding kinetics. VL - 13 SP - 822 KW - folding KW - theory AU - Weikl, TR AU - Palassini, M AU - Dill, KA PY - 2004/03// UR - http://dx.doi.org/10.1110/ps.03403604 ER -