| pubmed-article:16009941 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C0042295 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:16009941 | lifeskim:mentions | umls-concept:C1706536 | lld:lifeskim |
| pubmed-article:16009941 | pubmed:issue | 29 | lld:pubmed |
| pubmed-article:16009941 | pubmed:dateCreated | 2005-7-20 | lld:pubmed |
| pubmed-article:16009941 | pubmed:abstractText | Phi values are experimental measures of how the kinetics of protein folding is changed by single-site mutations. Phi values measure energetic quantities, but they are often interpreted in terms of the structures of the transition-state ensemble. Here, we describe a simple analytical model of the folding kinetics in terms of the formation of protein substructures. The model shows that Phi values have both structural and energetic components. It also provides a natural and general interpretation of "nonclassical" Phi values (i.e., < 0 or > 1). The model reproduces the Phi values for 20 single-residue mutations in the alpha-helix of the protein CI2, including several nonclassical Phi values, in good agreement with experiments. | lld:pubmed |
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| pubmed-article:16009941 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16009941 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16009941 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16009941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16009941 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16009941 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16009941 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16009941 | pubmed:author | pubmed-author:DillKen AKA | lld:pubmed |
| pubmed-article:16009941 | pubmed:author | pubmed-author:WeiklThomas... | lld:pubmed |
| pubmed-article:16009941 | pubmed:author | pubmed-author:MerloClaudiaC | lld:pubmed |
| pubmed-article:16009941 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16009941 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:16009941 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:16009941 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16009941 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16009941 | pubmed:pagination | 10171-5 | lld:pubmed |
| pubmed-article:16009941 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:meshHeading | pubmed-meshheading:16009941... | lld:pubmed |
| pubmed-article:16009941 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16009941 | pubmed:articleTitle | Phi values in protein-folding kinetics have energetic and structural components. | lld:pubmed |
| pubmed-article:16009941 | pubmed:affiliation | Max Planck Institute of Colloids and Interfaces, Theory Division, 14424 Potsdam, Germany. | lld:pubmed |
| pubmed-article:16009941 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16009941 | pubmed:publicationType | Comparative Study | lld:pubmed |
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