Fast protein folding kinetics Export

@article{citeulike:6012082, abstract = {10.1073/pnas.1735417100 Proteins are complex molecules, yet their folding kinetics is often fast (microseconds) and simple, involving only a single exponential function of time (called two-state kinetics). The main model for two-state kinetics has been transition-state theory, where an energy barrier defines a slow step to reach an improbable structure. But how can barriers explain fast processes, such as folding? We study a simple model with rigorous kinetics that explains the high speed instead as a result of the microscopic parallelization of folding trajectories. The single exponential results from a separation of timescales; the parallelization of routes is high at the start of folding and low thereafter. The ensemble of rate-limiting chain conformations is different from in transition-state theory; it is broad, overlaps with the denatured state, is not aligned along a single reaction coordinate, and involves well populated, rather than improbable, structures.}, author = {Schonbrun, Jack and Dill, Ken A.}, citeulike-article-id = {6012082}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.1735417100}, citeulike-linkout-1 = {http://www.pnas.org/content/100/22/12678.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/100/22/12678.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/14569019}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=14569019}, day = {28}, doi = {10.1073/pnas.1735417100}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {folding}, month = {October}, number = {22}, pages = {12678--12682}, posted-at = {2009-10-26 17:26:34}, priority = {0}, title = {Fast protein folding kinetics}, url = {http://dx.doi.org/10.1073/pnas.1735417100}, volume = {100}, year = {2003} }

TY - JOUR ID - citeulike:6012082 L3 - citeulike-article-id:6012082 N2 - 10.1073/pnas.1735417100 Proteins are complex molecules, yet their folding kinetics is often fast (microseconds) and simple, involving only a single exponential function of time (called two-state kinetics). The main model for two-state kinetics has been transition-state theory, where an energy barrier defines a slow step to reach an improbable structure. But how can barriers explain fast processes, such as folding? We study a simple model with rigorous kinetics that explains the high speed instead as a result of the microscopic parallelization of folding trajectories. The single exponential results from a separation of timescales; the parallelization of routes is high at the start of folding and low thereafter. The ensemble of rate-limiting chain conformations is different from in transition-state theory; it is broad, overlaps with the denatured state, is not aligned along a single reaction coordinate, and involves well populated, rather than improbable, structures. IS - 22 JF - Proceedings of the National Academy of Sciences of the United States of America EP - 12682 TI - Fast protein folding kinetics VL - 100 SP - 12678 KW - folding AU - Schonbrun, Jack AU - Dill, Ken PY - 2003/10/28/ UR - http://dx.doi.org/10.1073/pnas.1735417100 ER -