Source:http://linkedlifedata.com/resource/pubmed/id/16481228
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2006-4-7
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pubmed:abstractText |
Pressure-jump induced relaxation kinetics can be used to study both protein unfolding and refolding. These processes can be initiated by upward and downward pressure-jumps of amplitudes of a few 10 to 100 MPa, with a dead-time on the order of milliseconds. In many cases, the relaxation times can be easily determined when the pressure cell is connected to a spectroscopic detection device, such as a spectrofluorimeter. Adiabatic heating or cooling can be limited by small pressure-jump amplitudes and a special design of the sample cell. Here, we discuss the application of this method to four proteins: 33-kDa and 23-kDa proteins from photo-system II, a variant of the green fluorescent protein, and a fluorescent variant of ribonuclease A. The thermodynamically predicted equivalency of upward and downward pressure-jump induced protein relaxation kinetics for typical two-state folders was observed for the 33-kDa protein, only. In contrast, the three other proteins showed significantly different kinetics for pressure-jumps in opposite directions. These results cannot be explained by sequential reaction schemes. Instead, they are in line with a more complex free energy landscape involving multiple pathways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Photosystem II Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease, Pancreatic
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1764
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
489-96
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16481228-Animals,
pubmed-meshheading:16481228-Cattle,
pubmed-meshheading:16481228-Green Fluorescent Proteins,
pubmed-meshheading:16481228-Kinetics,
pubmed-meshheading:16481228-Photosystem II Protein Complex,
pubmed-meshheading:16481228-Plant Proteins,
pubmed-meshheading:16481228-Pressure,
pubmed-meshheading:16481228-Protein Folding,
pubmed-meshheading:16481228-Ribonuclease, Pancreatic
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pubmed:year |
2006
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pubmed:articleTitle |
The use of pressure-jump relaxation kinetics to study protein folding landscapes.
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pubmed:affiliation |
INSERM U710, Université Montpellier 2, CC105, Place Eugène Bataillon, 34095 Montpellier Cédex 5, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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