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pubmed-article:18643017pubmed:dateCreated2008-7-22lld:pubmed
pubmed-article:18643017pubmed:abstractTextRecent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold. In this work, we present a force-dependent two-pathway four-state model to uniformly quantify these intriguing observations. Although our model is indistinguishable from the previous two-pathway three-state model in predicting the mean reduction rate, the distributions of dwell times of the two models are significantly distinctive. The very recent experiment favors our model.lld:pubmed
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pubmed-article:18643017pubmed:authorpubmed-author:Ou-YangZhong-...lld:pubmed
pubmed-article:18643017pubmed:authorpubmed-author:XueXiaochuanXlld:pubmed
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pubmed-article:18643017pubmed:year2008lld:pubmed
pubmed-article:18643017pubmed:articleTitleTwo-pathway four-state kinetic model of thioredoxin-catalyzed reduction of single forced disulfide bonds.lld:pubmed
pubmed-article:18643017pubmed:affiliationCenter for Advanced Study, Tsinghua University, Beijing 100084, China.lld:pubmed
pubmed-article:18643017pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18643017pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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