Source:http://linkedlifedata.com/resource/pubmed/id/14759171
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2004-2-4
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pubmed:abstractText |
The strength of a multimolecular system depends on the number of interactions that hold it together. Using dynamic force spectroscopy, we show how the kinetic stability of a system decreases as the number of molecular bonds is increased, as predicted by theory. The data raise important considerations for experimental tests of bond strength and, as a paradigm, suggest both routes to and pitfalls in methods for computational simulation of molecular transitions, such as ligand binding and protein folding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1318-9
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pubmed:dateRevised |
2008-1-17
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pubmed:meshHeading |
pubmed-meshheading:14759171-Biotin,
pubmed-meshheading:14759171-Kinetics,
pubmed-meshheading:14759171-Macromolecular Substances,
pubmed-meshheading:14759171-Microscopy, Atomic Force,
pubmed-meshheading:14759171-Serum Albumin, Bovine,
pubmed-meshheading:14759171-Structure-Activity Relationship,
pubmed-meshheading:14759171-Thermodynamics
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pubmed:year |
2004
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pubmed:articleTitle |
Influence of architecture on the kinetic stability of molecular assemblies.
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pubmed:affiliation |
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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