%0 Journal Article %1 ISI:000257178500001 %A Wallin, Stefan %A Shakhnovich, Eugene I. %C DIRAC HOUSE, TEMPLE BACK, BRISTOL BS1 6BE, ENGLAND %D 2008 %I IOP PUBLISHING LTD %J JOURNAL OF PHYSICS-CONDENSED MATTER %K review %N 28 %R 10.1088/0953-8984/20/28/283101 %T Understanding ensemble protein folding at atomic detail %V 20 %X Although far from routine, simulating the folding of specific short protein chains on the computer, at a detailed atomic level, is starting to become a reality. This remarkable progress, which has been made over the last decade or so, allows a fundamental aspect of the protein folding process to be addressed, namely its statistical nature. In order to make quantitative comparisons with experimental kinetic data a complete ensemble view of folding must be achieved, with key observables averaged over the large number of microscopically different folding trajectories available to a protein chain. Here we review recent advances in atomic-level protein folding simulations and the new insight provided by them into the protein folding process. An important element in understanding ensemble folding kinetics are methods for analyzing many separate folding trajectories, and we discuss techniques developed to condense the large amount of information contained in an ensemble of trajectories into a manageable picture of the folding process.

@article{ISI:000257178500001, abstract = {{Although far from routine, simulating the folding of specific short protein chains on the computer, at a detailed atomic level, is starting to become a reality. This remarkable progress, which has been made over the last decade or so, allows a fundamental aspect of the protein folding process to be addressed, namely its statistical nature. In order to make quantitative comparisons with experimental kinetic data a complete ensemble view of folding must be achieved, with key observables averaged over the large number of microscopically different folding trajectories available to a protein chain. Here we review recent advances in atomic-level protein folding simulations and the new insight provided by them into the protein folding process. An important element in understanding ensemble folding kinetics are methods for analyzing many separate folding trajectories, and we discuss techniques developed to condense the large amount of information contained in an ensemble of trajectories into a manageable picture of the folding process.}}, added-at = {2009-01-09T04:10:06.000+0100}, address = {{DIRAC HOUSE, TEMPLE BACK, BRISTOL BS1 6BE, ENGLAND}}, affiliation = {{Shakhnovich, EI (Reprint Author), Harvard Univ, Dept Chem \& Chem Biol, 12 Oxford St, Cambridge, MA 02138 USA. {[}Wallin, Stefan; Shakhnovich, Eugene I.] Harvard Univ, Dept Chem \& Chem Biol, Cambridge, MA 02138 USA.}}, article-number = {{283101}}, author = {Wallin, Stefan and Shakhnovich, Eugene I.}, author-email = {{eugene@belok.harvard.edu}}, biburl = {https://www.bibsonomy.org/bibtex/28c4d3b58f100435d078a953283d5807e/huiyangsfsu}, cited-references = {{ABKEVICH VI, 1994, BIOCHEMISTRY-US, V33, P10026. ALM E, 1999, P NATL ACAD SCI USA, V96, P11305. 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ZHOU RH, 2001, P NATL ACAD SCI USA, V98, P14931. ZHOU YQ, 1999, NATURE, V401, P400.}}, doc-delivery-number = {{319QJ}}, doi = {{10.1088/0953-8984/20/28/283101}}, interhash = {859466a288272e137990183908c2b41b}, intrahash = {8c4d3b58f100435d078a953283d5807e}, issn = {{0953-8984}}, journal = {{JOURNAL OF PHYSICS-CONDENSED MATTER}}, journal-iso = {{J. Phys.-Condes. Matter}}, keywords = {review}, keywords-plus = {{MOLECULAR-DYNAMICS SIMULATIONS; 3-HELIX BUNDLE PROTEIN; TRANSITION-STATE ENSEMBLE; SINGLE-DOMAIN PROTEINS; FREE-ENERGY LANDSCAPE; VILLIN HEADPIECE; CONTACT-ORDER; B-DOMAIN; HELICAL PROTEIN; CHYMOTRYPSIN INHIBITOR-2}}, language = {{English}}, month = {{JUL 16}}, number = {{28}}, number-of-cited-references = {{102}}, publisher = {{IOP PUBLISHING LTD}}, subject-category = {{Physics, Condensed Matter}}, times-cited = {{0}}, timestamp = {2009-01-09T04:10:07.000+0100}, title = {{Understanding ensemble protein folding at atomic detail}}, type = {{Review}}, unique-id = {{ISI:000257178500001}}, volume = {{20}}, year = {{2008}} }