Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1995-12-21
pubmed:abstractText
The pathway of protein folding is now being analyzed at the resolution of individual residues by kinetic measurements on suitably engineered mutants. The kinetic methods generally employed for studying folding are typically limited to the time range of > or = 1 ms because the folding of denatured proteins is usually initiated by mixing them with buffers that favor folding, and the dead time of rapid mixing experiments is about a millisecond. We now show that the study of protein folding may be extended to the microsecond time region by using temperature-jump measurements on the cold-unfolded state of a suitable protein. We are able to detect early events in the folding of mutants of barstar, the polypeptide inhibitor of barnase. A preliminary characterization of the fast phase from spectroscopic and phi-value analysis indicates that it is a transition between two relatively solvent-exposed states with little consolidation of structure.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-1318745, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-1390668, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-1569556, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-1641003, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-187215, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-2225910, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-2377205, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-2739734, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-2845278, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-2845279, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-3050134, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-3663627, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-3956736, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-4912353, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-5844452, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-7624336, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-7773750, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-7849030, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-7880824, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-7937967, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8043574, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8218183, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8265638, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8364032, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8476861, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-8513892, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479862-963241
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10668-72
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Submillisecond events in protein folding.
pubmed:affiliation
Cambridge University Chemical Laboratory, United Kingdom.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't