Linked Life Data

19751683

Source:http://linkedlifedata.com/resource/pubmed/id/19751683

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-9-15
pubmed:abstractText
The protein lambda(6-85) has been implicated in barrierless folding by observations of kinetic relaxation after nanosecond T-jump. In this work we observed folding of this protein after dilution of a high denaturant in an ultrarapid microfluidic mixer at temperatures far below the thermal midpoint. The observations of total intensity and spectral shift of tryptophan fluorescence yielded distinctly different kinetics and activation energies. These results may be explained as diffusion on a low-barrier, one-dimensional, free-energy surface, with different probes having different sensitivities along the reaction coordinate. Additionally, we observed an extremely fast phase within the mixing time that was not observed by T-jump, suggesting that the ensemble of unfolded states populated at high denaturant is distinct from those accessible at high temperature.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1542-0086
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1772-7
pubmed:dateRevised
2010-9-17
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Direct observation of downhill folding of lambda-repressor in a microfluidic mixer.
pubmed:affiliation
Department of Physics and Astronomy, Michigan State University, East Lansing, Michigan, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't