Source:http://linkedlifedata.com/resource/pubmed/id/21609875
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2011-5-25
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pubmed:abstractText |
Pressure perturbation calorimetry (PPC) is a new technique that makes possible to study the volumetric changes that occur upon protein unfolding. Here, we summarize the thermodynamic foundation of the method and introduce a two-state model for the analysis of the unfolding data monitored by PPC. Several examples of data analysis illustrating potential pitfalls and solutions are discussed.
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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:issn |
1557-7988
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
466
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-47
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pubmed:meshHeading |
pubmed-meshheading:21609875-Animals,
pubmed-meshheading:21609875-Calorimetry, Differential Scanning,
pubmed-meshheading:21609875-Equipment Design,
pubmed-meshheading:21609875-Humans,
pubmed-meshheading:21609875-Muramidase,
pubmed-meshheading:21609875-Pressure,
pubmed-meshheading:21609875-Protein Unfolding,
pubmed-meshheading:21609875-Proteins,
pubmed-meshheading:21609875-Ribonucleases,
pubmed-meshheading:21609875-Thermodynamics,
pubmed-meshheading:21609875-Ubiquitin
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pubmed:year |
2009
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pubmed:articleTitle |
Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins.
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pubmed:affiliation |
Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA.
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pubmed:publicationType |
Journal Article
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