Protein folding under confinement: A role for solvent Export

@article{citeulike:1380924, abstract = {10.1073/pnas.0608256104 Although most experimental and theoretical studies of protein folding involve proteins , the effects of spatial confinement may complicate protein folding . In this study, we examine the folding dynamics of villin (a small fast folding protein) with explicit solvent confined to an inert nanopore. We have calculated the probability of folding before unfolding ( ) under various confinement regimes. Using correlation techniques, we observed two competing effects. Confining protein alone promotes folding by destabilizing the unfolded state. In contrast, confining both protein and solvent gives rise to a solvent-mediated effect that destabilizes the native state. When both protein and solvent are confined we see unfolding to a compact unfolded state different from the unfolded state seen in bulk. Thus, we demonstrate that the confinement of solvent has a significant impact on protein kinetics and thermodynamics. We conclude with a discussion of the implications of these results for folding in confined environments such as the chaperonin cavity .}, author = {Lucent, Del and Vishal, V. and Pande, Vijay S.}, citeulike-article-id = {1380924}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0608256104}, citeulike-linkout-1 = {http://www.pnas.org/content/104/25/10430.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/104/25/10430.full.pdf}, citeulike-linkout-3 = {http://www.pnas.org/cgi/content/abstract/104/25/10430}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/17563390}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=17563390}, day = {19}, doi = {10.1073/pnas.0608256104}, journal = {Proceedings of the National Academy of Sciences}, keywords = {confinement, for\_ref, fullatom, md, simulation}, month = {June}, number = {25}, pages = {10430--10434}, posted-at = {2008-09-29 11:12:32}, priority = {3}, title = {Protein folding under confinement: A role for solvent}, url = {http://dx.doi.org/10.1073/pnas.0608256104}, volume = {104}, year = {2007} }

TY - JOUR ID - citeulike:1380924 L3 - citeulike-article-id:1380924 N2 - 10.1073/pnas.0608256104 Although most experimental and theoretical studies of protein folding involve proteins , the effects of spatial confinement may complicate protein folding . In this study, we examine the folding dynamics of villin (a small fast folding protein) with explicit solvent confined to an inert nanopore. We have calculated the probability of folding before unfolding ( ) under various confinement regimes. Using correlation techniques, we observed two competing effects. Confining protein alone promotes folding by destabilizing the unfolded state. In contrast, confining both protein and solvent gives rise to a solvent-mediated effect that destabilizes the native state. When both protein and solvent are confined we see unfolding to a compact unfolded state different from the unfolded state seen in bulk. Thus, we demonstrate that the confinement of solvent has a significant impact on protein kinetics and thermodynamics. We conclude with a discussion of the implications of these results for folding in confined environments such as the chaperonin cavity . IS - 25 JF - Proceedings of the National Academy of Sciences EP - 10434 TI - Protein folding under confinement: A role for solvent VL - 104 SP - 10430 KW - confinement KW - for_ref KW - fullatom KW - md KW - simulation AU - Lucent, Del AU - Vishal, V AU - Pande, Vijay PY - 2007/06/19/ UR - http://dx.doi.org/10.1073/pnas.0608256104 ER -