pubmed-article:7833803 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C1710706 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C0392762 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
pubmed-article:7833803 | lifeskim:mentions | umls-concept:C0052987 | lld:lifeskim |
pubmed-article:7833803 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:7833803 | pubmed:dateCreated | 1995-3-1 | lld:pubmed |
pubmed-article:7833803 | pubmed:abstractText | The fluorescence-monitored kinetics of folding and unfolding of barstar by guanidine hydrochloride (GdnHCl) in the folding transition zone, at pH 7, 25 degrees C, have been quantitatively analyzed using a 3-state mechanism: U(S)<-->UF<-->N. U(S) and UF are slow-refolding and fast-refolding unfolded forms of barstar, and N is the native protein. U(S) and UF probably differ in possessing trans and cis conformations, respectively, of the Tyr 47-Pro 48 bond. The 3-state model could be used because the kinetics of folding and unfolding of barstar show 2 phases, a fast phase and a slow phase, and because the relative amplitudes of the 2 phases depend only on the final refolding conditions and not on the initial conditions. Analysis of the observed kinetics according to the 3-state model yields the values of the 4 microscopic rate constants that describe the transitions between the 3 states at different concentrations of GdnHCl. The value of the equilibrium unfolded ratio U(S):UF (K21) and the values of the rate constants of the U(S)-->UF and UF-->U(S) reactions, k12 and k21, respectively, are shown to be independent of the concentration of GdnHCl. K21 has a value of 2.1 +/- 0.1, and k12 and k21 have values of 5.3 x 10(-3) s-1 and 11.2 x 10(-3) s-1, respectively. Double-jump experiments that monitor reactions that are silent to fluorescence monitoring were used to confirm the values of K21, k12, and k21 obtained from the 3-state analysis and thereby the validity of the 3-state model.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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pubmed-article:7833803 | pubmed:language | eng | lld:pubmed |
pubmed-article:7833803 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7833803 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7833803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7833803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7833803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7833803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7833803 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7833803 | pubmed:month | Sep | lld:pubmed |
pubmed-article:7833803 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:7833803 | pubmed:author | pubmed-author:UdgaonkarJ... | lld:pubmed |
pubmed-article:7833803 | pubmed:author | pubmed-author:ShastryM CMC | lld:pubmed |
pubmed-article:7833803 | pubmed:author | pubmed-author:AgasheV RVR | lld:pubmed |
pubmed-article:7833803 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7833803 | pubmed:volume | 3 | lld:pubmed |
pubmed-article:7833803 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7833803 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7833803 | pubmed:pagination | 1409-17 | lld:pubmed |
pubmed-article:7833803 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:7833803 | pubmed:meshHeading | pubmed-meshheading:7833803-... | lld:pubmed |
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pubmed-article:7833803 | pubmed:meshHeading | pubmed-meshheading:7833803-... | lld:pubmed |
pubmed-article:7833803 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7833803 | pubmed:articleTitle | Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone. | lld:pubmed |
pubmed-article:7833803 | pubmed:affiliation | National Centre For Biological Sciences, TIFR Centre, Indian Institute of Science Campus, Bangalore. | lld:pubmed |
pubmed-article:7833803 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7833803 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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