pubmed-article:8673605 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8673605 | lifeskim:mentions | umls-concept:C0014653 | lld:lifeskim |
pubmed-article:8673605 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
pubmed-article:8673605 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
pubmed-article:8673605 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:8673605 | lifeskim:mentions | umls-concept:C0052218 | lld:lifeskim |
pubmed-article:8673605 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:8673605 | pubmed:dateCreated | 1996-8-15 | lld:pubmed |
pubmed-article:8673605 | pubmed:abstractText | Little is known about the kinetic process in which stable intermediates in protein folding are formed: whether their folding is highly cooperative (two-state) or weakly cooperative is controversial. We report here that the folding and unfolding kinetics of the pH 4-stable intermediate (I1) of apomyoglobin are measurable, in the millisecond time range, when monitored by stopped-flow measurements of tryptophan fluorescence. The kinetics confirm that folding of I1 is strongly cooperative, but there is a burst phase (missing amplitude) in unfolding. If the faster steps in unfolding of I1 can be measured directly by suitable fast-reaction methods, they will give information about the nature of the folding transition. | lld:pubmed |
pubmed-article:8673605 | pubmed:language | eng | lld:pubmed |
pubmed-article:8673605 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673605 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8673605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8673605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673605 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8673605 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8673605 | pubmed:issn | 1072-8368 | lld:pubmed |
pubmed-article:8673605 | pubmed:author | pubmed-author:BaldwinR LRL | lld:pubmed |
pubmed-article:8673605 | pubmed:author | pubmed-author:JaminMM | lld:pubmed |
pubmed-article:8673605 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8673605 | pubmed:volume | 3 | lld:pubmed |
pubmed-article:8673605 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8673605 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8673605 | pubmed:pagination | 613-8 | lld:pubmed |
pubmed-article:8673605 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:meshHeading | pubmed-meshheading:8673605-... | lld:pubmed |
pubmed-article:8673605 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8673605 | pubmed:articleTitle | Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. | lld:pubmed |
pubmed-article:8673605 | pubmed:affiliation | Department of Biochemistry, Stanford University Medical Center, California 94305-5307, USA. | lld:pubmed |
pubmed-article:8673605 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8673605 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8673605 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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