| pubmed-article:9162943 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9162943 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9162943 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:9162943 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:9162943 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:9162943 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:9162943 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9162943 | pubmed:dateCreated | 1997-5-28 | lld:pubmed |
| pubmed-article:9162943 | pubmed:abstractText | To determine when secondary structure forms as two chains coalesce to form an alpha-helical dimer, the folding rates of variants of the coiled coil region of GCN4 were compared. Residues at non-perturbing positions along the exterior length of the helices were substituted one at a time with alanine and glycine to vary helix propensity and therefore dimer stability. For all variants, the bimolecular folding rate remains largely unchanged; the unfolding rate changes to largely account for the change in stability. Thus, contrary to most folding models, widespread helix is not yet formed at the rate-limiting step in the folding pathway. The high-energy transition state is a collapsed form that contains little if any secondary structure, as suggested for the globular protein cytochrome c (Sosnick et al., Proteins 24: 413-426, 1996). | lld:pubmed |
| pubmed-article:9162943 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9162943 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9162943 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9162943 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9162943 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9162943 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9162943 | pubmed:issn | 0887-3585 | lld:pubmed |
| pubmed-article:9162943 | pubmed:author | pubmed-author:EnglanderS... | lld:pubmed |
| pubmed-article:9162943 | pubmed:author | pubmed-author:JacksonSS | lld:pubmed |
| pubmed-article:9162943 | pubmed:author | pubmed-author:DeGradoW FWF | lld:pubmed |
| pubmed-article:9162943 | pubmed:author | pubmed-author:WilkR RRR | lld:pubmed |
| pubmed-article:9162943 | pubmed:author | pubmed-author:SosnickT RTR | lld:pubmed |
| pubmed-article:9162943 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9162943 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:9162943 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9162943 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9162943 | pubmed:pagination | 427-32 | lld:pubmed |
| pubmed-article:9162943 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:meshHeading | pubmed-meshheading:9162943-... | lld:pubmed |
| pubmed-article:9162943 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:9162943 | pubmed:articleTitle | The role of helix formation in the folding of a fully alpha-helical coiled coil. | lld:pubmed |
| pubmed-article:9162943 | pubmed:affiliation | The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059, USA. | lld:pubmed |
| pubmed-article:9162943 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9162943 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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