Source:http://linkedlifedata.com/resource/pubmed/id/16683786
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
2006-5-10
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| pubmed:abstractText |
In striking contrast to simple polymer physics theory, which does not account for solvent effects, we find that physical confinement of solvated biopolymers decreases solvent entropy, which in turn leads to a reduction in the organized structural content of the polymer. Since our theory is based on a fundamental property of water-protein statistical mechanics, we expect it to have broad implications in many biological and material science contexts.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0002-7863
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
128
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6316-7
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| pubmed:dateRevised |
2008-1-17
|
| pubmed:meshHeading |
pubmed-meshheading:16683786-Entropy,
pubmed-meshheading:16683786-Models, Molecular,
pubmed-meshheading:16683786-Nanotubes, Carbon,
pubmed-meshheading:16683786-Protein Denaturation,
pubmed-meshheading:16683786-Protein Structure, Secondary,
pubmed-meshheading:16683786-Proteins,
pubmed-meshheading:16683786-Solvents
|
| pubmed:year |
2006
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| pubmed:articleTitle |
Nanotube confinement denatures protein helices.
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| pubmed:affiliation |
Department of Chemistry, Stanford University, Stanford, California 94305-5080, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|