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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-12-30
pubmed:abstractText
Folding and unfolding rates have been measured for the peripheral subunit-binding domain, a small three-helix protein. The protein folds very fast, with rates too rapid to be measured using traditional stopped-flow techniques. Folding and unfolding rates were measured as a function of temperature using dynamic NMR lineshape analysis. At the lowest temperature at which there is sufficient broadening to measure rates, 41 degrees C, the folding rate is 16,050 s(-1). Thus, the halftime required for folding is 43 micros. At the same temperature, the unfolding rate is 2800 s(-1). Identical rates were measured using resolved resonances from Val16 in the loop and Val21 at the end of the 310-helix. Folding rates have been correlated with protein topology, and this correlation is consistent with the rapid folding of the peripheral subunit-binding domain. The results presented here show that the peripheral subunit-binding domain is the third fastest folding protein for which rates have been estimated. The folding rate is the fastest that has been directly measured and provides further support for the importance of chain topology as a major determinant of folding rates.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
763-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Submillisecond folding of the peripheral subunit-binding domain.
pubmed:affiliation
Department of Physiology and Biophysics, SUNY Stony Brook, Stony Brook, NY 11794-8661, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't