Submillisecond kinetics of protein folding

by: William A Eaton, Victor Munoz, Peggy A Thompson, Chi-Kin Chan, James Hofrichter

Current Opinion in Structural Biology, Vol. 7, No. 1. (February 1997), pp. 10-14.

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摘要

New experimental methods permit observation of protein folding and unfolding on the previously inaccessible nanosecond--microsecond timescale. These studies are beginning to establish times for the elementary motions in protein folding -- secondary structure and loop formation, local hydrophobic collapse, and global collapse to the compact denatured state. They permit an estimate of about one microsecond for the shortest time in which a protein can possibly fold.

@article{citeulike:2281182, abstract = {New experimental methods permit observation of protein folding and unfolding on the previously inaccessible nanosecond--microsecond timescale. These studies are beginning to establish times for the elementary motions in protein folding -- secondary structure and loop formation, local hydrophobic collapse, and global collapse to the compact denatured state. They permit an estimate of about one microsecond for the shortest time in which a protein can possibly fold.}, author = {Eaton, William A. and Munoz, Victor and Thompson, Peggy A. and Chan, Chi-Kin and Hofrichter, James }, citeulike-article-id = {2281182}, doi = {http://dx.doi.org/10.1016/S0959-440X(97)80003-6}, journal = {Current Opinion in Structural Biology}, keywords = {folding, hbproject, hydrophobicity, proteins, review, secondary-structures}, month = {February}, number = {1}, pages = {10--14}, posted-at = {2008-01-23 17:03:09}, priority = {2}, title = {Submillisecond kinetics of protein folding}, url = {http://dx.doi.org/10.1016/S0959-440X(97)80003-6}, volume = {7}, year = {1997} }

RIS record

TY - JOUR ID - citeulike:2281182 L3 - citeulike-article-id:2281182 TI - Submillisecond kinetics of protein folding JF - Current Opinion in Structural Biology VL - 7 IS - 1 SP - 10 EP - 14 N2 - New experimental methods permit observation of protein folding and unfolding on the previously inaccessible nanosecond--microsecond timescale. These studies are beginning to establish times for the elementary motions in protein folding -- secondary structure and loop formation, local hydrophobic collapse, and global collapse to the compact denatured state. They permit an estimate of about one microsecond for the shortest time in which a protein can possibly fold. KW - folding KW - hbproject KW - hydrophobicity KW - proteins KW - review KW - secondary-structures AU - Eaton, William AU - Munoz, Victor AU - Thompson, Peggy AU - Chan, Chi-Kin AU - Hofrichter, James PY - 1997/02// UR - http://dx.doi.org/10.1016/S0959-440X(97)80003-6 ER -

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