| pubmed-article:18096639 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18096639 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:18096639 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18096639 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:18096639 | lifeskim:mentions | umls-concept:C0380479 | lld:lifeskim |
| pubmed-article:18096639 | lifeskim:mentions | umls-concept:C0598447 | lld:lifeskim |
| pubmed-article:18096639 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18096639 | pubmed:dateCreated | 2008-1-29 | lld:pubmed |
| pubmed-article:18096639 | pubmed:abstractText | Homodimeric archaeal histones and heterodimeric eukaryotic histones share a conserved structure but fold through different kinetic mechanisms, with a correlation between faster folding/association rates and the population of kinetic intermediates. Wild-type hMfB (from Methanothermus fervidus) has no intrinsic fluorophores; Met35, which is Tyr in hyperthermophilic archaeal histones such as hPyA1 (from Pyrococcus strain GB-3A), was mutated to Tyr and Trp. Two Tyr-to-Trp mutants of hPyA1 were also characterized. All fluorophores were introduced into the long, central alpha-helix of the histone fold. Far-UV circular dichroism (CD) indicated that the fluorophores did not significantly alter the helical content of the histones. The equilibrium unfolding transitions of the histone variants were two-state, reversible processes, with DeltaG degrees (H2O) values within 1 kcal/mol of the wild-type dimers. The hPyA1 Trp variants fold by two-state kinetic mechanisms like wild-type hPyA1, but with increased folding and unfolding rates, suggesting that the mutated residues (Tyr-32 and Tyr-36) contribute to transition state structure. Like wild-type hMfB, M35Y and M35W hMfB fold by a three-state mechanism, with a stopped-flow CD burst-phase monomeric intermediate. The M35 mutants populate monomeric intermediates with increased secondary structure and stability but exhibit decreased folding rates; this suggests that nonnative interactions occur from burial of the hydrophobic Tyr and Trp residues in this kinetic intermediate. These results implicate the long central helix as a key component of the structure in the kinetic monomeric intermediates of hMfB as well as the dimerization transition state in the folding of hPyA1. | lld:pubmed |
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| pubmed-article:18096639 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18096639 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096639 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18096639 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18096639 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18096639 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:18096639 | pubmed:author | pubmed-author:GlossLisa MLM | lld:pubmed |
| pubmed-article:18096639 | pubmed:author | pubmed-author:StumpMatthew... | lld:pubmed |
| pubmed-article:18096639 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18096639 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:18096639 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18096639 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18096639 | pubmed:pagination | 322-32 | lld:pubmed |
| pubmed-article:18096639 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
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| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
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| pubmed-article:18096639 | pubmed:meshHeading | pubmed-meshheading:18096639... | lld:pubmed |
| pubmed-article:18096639 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18096639 | pubmed:articleTitle | Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediate. | lld:pubmed |
| pubmed-article:18096639 | pubmed:affiliation | School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, USA. | lld:pubmed |
| pubmed-article:18096639 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18096639 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18096639 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18096639 | lld:pubmed |
