Protein folding theory: from lattice to all-atom models. Export

@article{citeulike:334781, abstract = {This review focuses on recent advances in understanding protein folding kinetics in the context of nucleation theory. We present basic concepts such as nucleation, folding nucleus, and transition state ensemble and then discuss recent advances and challenges in theoretical understanding of several key aspects of protein folding kinetics. We cover recent topology-based approaches as well as evolutionary studies and molecular dynamics approaches to determine protein folding nucleus and analyze other aspects of folding kinetics. Finally, we briefly discuss successful all-atom Monte-Carlo simulations of protein folding and conclude with a brief outlook for the future.}, address = {Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. leonid@origami.harvard.edu}, author = {Mirny, L. and Shakhnovich, E.}, citeulike-article-id = {334781}, citeulike-linkout-0 = {http://dx.doi.org/10.1146/annurev.biophys.30.1.361}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11340064}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11340064}, doi = {10.1146/annurev.biophys.30.1.361}, issn = {1056-8700}, journal = {Annu Rev Biophys Biomol Struct}, pages = {361--396}, posted-at = {2006-09-29 11:10:03}, priority = {2}, title = {Protein folding theory: from lattice to all-atom models.}, url = {http://dx.doi.org/10.1146/annurev.biophys.30.1.361}, volume = {30}, year = {2001} }

TY - JOUR ID - citeulike:334781 L3 - citeulike-article-id:334781 N2 - This review focuses on recent advances in understanding protein folding kinetics in the context of nucleation theory. We present basic concepts such as nucleation, folding nucleus, and transition state ensemble and then discuss recent advances and challenges in theoretical understanding of several key aspects of protein folding kinetics. We cover recent topology-based approaches as well as evolutionary studies and molecular dynamics approaches to determine protein folding nucleus and analyze other aspects of folding kinetics. Finally, we briefly discuss successful all-atom Monte-Carlo simulations of protein folding and conclude with a brief outlook for the future. JF - Annu Rev Biophys Biomol Struct SN - 1056-8700 AD - Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. leonid@origami.harvard.edu EP - 396 TI - Protein folding theory: from lattice to all-atom models. VL - 30 SP - 361 AU - Mirny, L AU - Shakhnovich, E PY - 2001/// UR - http://dx.doi.org/10.1146/annurev.biophys.30.1.361 ER -