| pubmed-article:8495202 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8495202 | lifeskim:mentions | umls-concept:C0025965 | lld:lifeskim |
| pubmed-article:8495202 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:8495202 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:8495202 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8495202 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8495202 | pubmed:dateCreated | 1993-6-24 | lld:pubmed |
| pubmed-article:8495202 | pubmed:abstractText | Thermally unfolded staphylococcal nuclease has been rapidly quenched to temperatures near 0 degree C and the refolding behavior examined using an NMR kinetic experiment. Unfolded protein, exhibiting random coil chemical shifts, persists following the quench and refolds in two distinct kinetic phases. A protein folding intermediate with a trans Lys 116-Pro 117 peptide bond is transiently overpopulated and relaxes to the predominantly cis native cis-trans equilibrium. The rate of trans-->cis isomerization in the native-like nuclease intermediate is approximately 100-fold faster than that observed in a Lys-Pro model peptide. The activation enthalpy of 20 kcal/mol observed for the nuclease Lys 116-Pro 117 peptide bond is comparable to that observed for other X-Pro isomerizations. | lld:pubmed |
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| pubmed-article:8495202 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8495202 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8495202 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8495202 | pubmed:month | May | lld:pubmed |
| pubmed-article:8495202 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8495202 | pubmed:author | pubmed-author:JayG EGE | lld:pubmed |
| pubmed-article:8495202 | pubmed:author | pubmed-author:KautzR ARA | lld:pubmed |
| pubmed-article:8495202 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8495202 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:8495202 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8495202 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8495202 | pubmed:pagination | 851-8 | lld:pubmed |
| pubmed-article:8495202 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8495202 | pubmed:meshHeading | pubmed-meshheading:8495202-... | lld:pubmed |
| pubmed-article:8495202 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8495202 | pubmed:articleTitle | NMR analysis of staphylococcal nuclease thermal quench refolding kinetics. | lld:pubmed |
| pubmed-article:8495202 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511. | lld:pubmed |
| pubmed-article:8495202 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8495202 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8495202 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8495202 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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