| pubmed-article:15037063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15037063 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:15037063 | lifeskim:mentions | umls-concept:C0184512 | lld:lifeskim |
| pubmed-article:15037063 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:15037063 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:15037063 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15037063 | pubmed:dateCreated | 2004-3-23 | lld:pubmed |
| pubmed-article:15037063 | pubmed:abstractText | Double mutant cycle analysis was employed to ascertain the role of intra- and interchain salt-bridges in the folding and stability of the dimeric coiled-coil peptide, GCN4-p1, the 33-residue leucine zipper domain of the transcriptional activator GCN4. Equilibrium circular dichroism studies of the urea-induced unfolding reaction at neutral pH revealed that both types of ionic interactions, localized primarily in the N-terminal portion of the molecule, enhance the stability of the native coiled-coil. By contrast, comparable stopped-flow circular dichroism studies indicate that the salt-bridge interactions, with one possible exception, are not well formed in the transition state for folding. Although the E22Q/R25A double mutant failed to fold, fragmentation studies suggest that the E22/R25 intramolecular salt-bridge may play a critical role in stabilizing C-terminal nascent helices that drive the association reaction. The remaining salt-bridges appear to stabilize the parallel-stranded coiled-coil architecture of GCN4-p1 only after the peptide traverses the rate-limiting, dimeric transition state. | lld:pubmed |
| pubmed-article:15037063 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15037063 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15037063 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15037063 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15037063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15037063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15037063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15037063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15037063 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15037063 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15037063 | pubmed:author | pubmed-author:MatthewsC... | lld:pubmed |
| pubmed-article:15037063 | pubmed:author | pubmed-author:Ibarra-Molero... | lld:pubmed |
| pubmed-article:15037063 | pubmed:author | pubmed-author:ZitzewitzJill... | lld:pubmed |
| pubmed-article:15037063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15037063 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:15037063 | pubmed:volume | 336 | lld:pubmed |
| pubmed-article:15037063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15037063 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15037063 | pubmed:pagination | 989-96 | lld:pubmed |
| pubmed-article:15037063 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
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| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
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| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:meshHeading | pubmed-meshheading:15037063... | lld:pubmed |
| pubmed-article:15037063 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15037063 | pubmed:articleTitle | Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. | lld:pubmed |
| pubmed-article:15037063 | pubmed:affiliation | Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. | lld:pubmed |
| pubmed-article:15037063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15037063 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15037063 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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