Analysis of the Free-Energy Surface of Proteins from Reversible Folding Simulations Export

@article{citeulike:5104867, abstract = {Author Summary The process of protein folding is a complex transition from a disordered to an ordered state. Here, we simulate a specific fast-folding protein at the point at which the native and denatured states are at equilibrium and show that obtaining an accurate description of the mechanisms of folding and unfolding is far from trivial. Using simple quantities which quantify the degree of native order is, in the case of this protein, clearly misleading. We show that an unbiased representation of the free-energy surface can be obtained; using such a representation we are able to redesign the landscape and thus modify, upon site-specific "mutations", the folding and unfolding rates. This leads us to formulate a hypothesis to explain the very fast folding of many proteins.}, author = {Allen, Lucy R. and Krivov, Sergei V. and Paci, Emanuele}, citeulike-article-id = {5104867}, citeulike-linkout-0 = {http://dx.doi.org/10.1371/journal.pcbi.1000428}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19593364}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19593364}, day = {10}, doi = {10.1371/journal.pcbi.1000428}, issn = {1553-7358}, journal = {PLoS Comput Biol}, keywords = {dihedral, free-energy, short-peptides}, month = {July}, number = {7}, pages = {e1000428+}, posted-at = {2009-07-10 11:52:24}, priority = {2}, publisher = {Public Library of Science}, title = {Analysis of the Free-Energy Surface of Proteins from Reversible Folding Simulations}, url = {http://dx.doi.org/10.1371/journal.pcbi.1000428}, volume = {5}, year = {2009} }

TY - JOUR ID - citeulike:5104867 L3 - citeulike-article-id:5104867 N2 - Author Summary The process of protein folding is a complex transition from a disordered to an ordered state. Here, we simulate a specific fast-folding protein at the point at which the native and denatured states are at equilibrium and show that obtaining an accurate description of the mechanisms of folding and unfolding is far from trivial. Using simple quantities which quantify the degree of native order is, in the case of this protein, clearly misleading. We show that an unbiased representation of the free-energy surface can be obtained; using such a representation we are able to redesign the landscape and thus modify, upon site-specific "mutations", the folding and unfolding rates. This leads us to formulate a hypothesis to explain the very fast folding of many proteins. IS - 7 JF - PLoS Comput Biol SN - 1553-7358 TI - Analysis of the Free-Energy Surface of Proteins from Reversible Folding Simulations PB - Public Library of Science VL - 5 SP - e1000428 KW - dihedral KW - free-energy KW - short-peptides AU - Allen, Lucy AU - Krivov, Sergei AU - Paci, Emanuele PY - 2009/07/10/ UR - http://dx.doi.org/10.1371/journal.pcbi.1000428 ER -