pubmed-article:10074340 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10074340 | lifeskim:mentions | umls-concept:C0444706 | lld:lifeskim |
pubmed-article:10074340 | lifeskim:mentions | umls-concept:C0449851 | lld:lifeskim |
pubmed-article:10074340 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:10074340 | lifeskim:mentions | umls-concept:C0439224 | lld:lifeskim |
pubmed-article:10074340 | lifeskim:mentions | umls-concept:C0599489 | lld:lifeskim |
pubmed-article:10074340 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:10074340 | pubmed:dateCreated | 1999-3-23 | lld:pubmed |
pubmed-article:10074340 | pubmed:abstractText | A pressure-jump apparatus was employed in investigating the kinetics of protein unfolding and refolding. In the reaction cell, the pressure can be increased or decreased by 100-160 bar within 50-100 microseconds and then held constant. Thus, unfolding and refolding reactions in the time range from 70 microseconds to 70 s can be followed with this technique. Measurements are possible in the transition regions of thermally or denaturant-induced folding in a wide range of temperatures and solvent conditions. We used this pressure-jump method to determine the temperature dependence of the rate constants of unfolding and refolding of the cold shock protein of Bacillus subtilis and of three variants thereof with Phe --> Ala substitutions in the central beta-sheet region. For all variants, the change in heat capacity occurred in refolding between the unfolded and activated states, suggesting that the overall native-like character of the activated state of folding was not changed by the deletion of individual Phe side chains. The Phe27Ala mutation affected the rate of unfolding only; the Phe15Ala and Phe17Ala mutations changed the kinetics of both unfolding and refolding. Although the activated state of folding of the cold shock protein is overall native-like, individual side chains are still in a non-native environment. | lld:pubmed |
pubmed-article:10074340 | pubmed:language | eng | lld:pubmed |
pubmed-article:10074340 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10074340 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10074340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10074340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10074340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10074340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10074340 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10074340 | pubmed:month | Mar | lld:pubmed |
pubmed-article:10074340 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:PeriGG | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:SchmidF XFX | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:GeevesM AMA | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:JacobMM | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:HoltermannGG | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:ReinsteinJJ | lld:pubmed |
pubmed-article:10074340 | pubmed:author | pubmed-author:SchindlerTT | lld:pubmed |
pubmed-article:10074340 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10074340 | pubmed:day | 9 | lld:pubmed |
pubmed-article:10074340 | pubmed:volume | 38 | lld:pubmed |
pubmed-article:10074340 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10074340 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10074340 | pubmed:pagination | 2882-91 | lld:pubmed |
pubmed-article:10074340 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:10074340 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10074340 | pubmed:articleTitle | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | lld:pubmed |
pubmed-article:10074340 | pubmed:affiliation | Biochemisches Laboratorium, Universität Bayreuth, Germany. | lld:pubmed |
pubmed-article:10074340 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10074340 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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