| pubmed-article:1525171 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C0035541 | lld:lifeskim |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C1609982 | lld:lifeskim |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C1333134 | lld:lifeskim |
| pubmed-article:1525171 | lifeskim:mentions | umls-concept:C0439534 | lld:lifeskim |
| pubmed-article:1525171 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:1525171 | pubmed:dateCreated | 1992-10-16 | lld:pubmed |
| pubmed-article:1525171 | pubmed:abstractText | Using small-angle X-ray scattering and Fourier transform infrared spectroscopy, we have determined that the thermally denatured state of native ribonuclease A is on average a compact structure having residual secondary structure. Under strongly reducing conditions, the protein further unfolds into a looser structure with larger dimensions but still retains a comparable amount of secondary structure. The dimensions of the thermally and chemically denatured states of the reduced protein are different but both are more compact than is predicted for a random coil of the same length. These results demonstrate that thermal denaturation in ribonuclease A is not a simple two-state transition from a native to a completely disordered random coil state. | lld:pubmed |
| pubmed-article:1525171 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1525171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1525171 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1525171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1525171 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1525171 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1525171 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1525171 | pubmed:author | pubmed-author:TrewhellaJJ | lld:pubmed |
| pubmed-article:1525171 | pubmed:author | pubmed-author:SosnickT RTR | lld:pubmed |
| pubmed-article:1525171 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1525171 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:1525171 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:1525171 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1525171 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1525171 | pubmed:pagination | 8329-35 | lld:pubmed |
| pubmed-article:1525171 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1525171 | pubmed:meshHeading | pubmed-meshheading:1525171-... | lld:pubmed |
| pubmed-article:1525171 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1525171 | pubmed:articleTitle | Denatured states of ribonuclease A have compact dimensions and residual secondary structure. | lld:pubmed |
| pubmed-article:1525171 | pubmed:affiliation | Life Sciences Division, Los Alamos National Laboratory, New Mexico 87545. | lld:pubmed |
| pubmed-article:1525171 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1525171 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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