| pubmed-article:8841145 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8841145 | lifeskim:mentions | umls-concept:C0035541 | lld:lifeskim |
| pubmed-article:8841145 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:8841145 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:8841145 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:8841145 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:8841145 | pubmed:issue | 39 | lld:pubmed |
| pubmed-article:8841145 | pubmed:dateCreated | 1996-11-12 | lld:pubmed |
| pubmed-article:8841145 | pubmed:abstractText | Tryptophan was substituted for Tyr92 to create a sensitive and unique optical probe in order to study the unfolding and refolding kinetics of disulfide-intact bovine pancreatic ribonuclease A by fluorescence-detected stopped-flow techniques. The stability of the Trp mutant was found to be similar to that of wild-type RNase A when denatured by heat or GdnHCl, and the mutant was found to have 85% of the activity of the wild-type protein. Single-jump unfolding experiments showed that the unfolding pathway of the Trp mutant contains a fast and a slow phase similar to those seen previously for the wild-type protein, indicating that the mutation did not alter the unfolding pathway significantly. The activation energy of the slow-unfolding phase suggested that proline isomerization is involved, with the Trp residue presumably reporting on changes in its local environment. Single-jump refolding experiments revealed the presence of GdnHCl-independent burst phase and a native-like intermediate, most likely IN, on the folding pathway. Single-jump refolding data at various final GdnHCl concentrations were fit to a kinetic folding model involving two pathways to the native state; one pathway involves the intermediate IN, and the other is a direct one to the native state. This model provides site-specific information, since Trp92 monitors the formation of local structure only in the neighborhood of that residue. Double-jump refolding experiments permitted the detection of a previously reported, hydrophobically collapsed intermediate, I phi. The refolding data support the hypothesis that the region around position 92 is a chain-folding initiation site in the folding pathway. | lld:pubmed |
| pubmed-article:8841145 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8841145 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8841145 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8841145 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8841145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8841145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8841145 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8841145 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8841145 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8841145 | pubmed:author | pubmed-author:ScheragaH AHA | lld:pubmed |
| pubmed-article:8841145 | pubmed:author | pubmed-author:RothwarfD MDM | lld:pubmed |
| pubmed-article:8841145 | pubmed:author | pubmed-author:HouryW AWA | lld:pubmed |
| pubmed-article:8841145 | pubmed:author | pubmed-author:SendakR ARA | lld:pubmed |
| pubmed-article:8841145 | pubmed:author | pubmed-author:WedemeyerW... | lld:pubmed |
| pubmed-article:8841145 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8841145 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8841145 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:8841145 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8841145 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8841145 | pubmed:pagination | 12978-92 | lld:pubmed |
| pubmed-article:8841145 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8841145 | pubmed:meshHeading | pubmed-meshheading:8841145-... | lld:pubmed |
| pubmed-article:8841145 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8841145 | pubmed:articleTitle | Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A. | lld:pubmed |
| pubmed-article:8841145 | pubmed:affiliation | Baker Laboratory of Chemistry, Cornell University, Ithaca, New York 14853-1301, USA. | lld:pubmed |
| pubmed-article:8841145 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8841145 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8841145 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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