Linked Life Data

18643017

Source:http://linkedlifedata.com/resource/pubmed/id/18643017

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5 Pt 1
pubmed:dateCreated
2008-7-22
pubmed:abstractText
Recent 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1539-3755
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
050903
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Two-pathway four-state kinetic model of thioredoxin-catalyzed reduction of single forced disulfide bonds.
pubmed:affiliation
Center for Advanced Study, Tsinghua University, Beijing 100084, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't