Linked Life Data

9063471

Source:http://linkedlifedata.com/resource/pubmed/id/9063471

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-4-7
pubmed:abstractText
The kinetics of the unfolding and refolding of the myosin rod have been studied by fluorescence and circular dichroism techniques, at different concentrations of protein and guanidine hydrochloride. The unfolding of the myosin rod was fast and at least biphasic in 2-3 M denaturant, with an initial immediate phase followed by a slower low-amplitude first-order phase. The refolding of the rod in 0.4-2 M guanidine hydrochloride was also at least biphasic; an initial immediate phase preceded a slow second-order phase. At the final denaturant concentration of 0.8 M, the amplitude of the burst phase was weakly dependent on the protein concentration and the rate constant of the refolding slow phase was optimal. These data are incorporated into a folding mechanism with at least three states. The high rates of the first steps of unfolding and refolding may be relevant for the functioning of the native myosin molecule by allowing a transient separation of the two strands of the myosin tail.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
244
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Kinetics of folding of the myosin rod.
pubmed:affiliation
Laboratoire des Protéines et Génes Musculaires, Unité associée au CNRS 1131, Université de Paris-Sud, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't