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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2004-4-27
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pubmed:abstractText |
A major result of incoherent elastic neutron-scattering experiments on protein powders is the strong dependence of the intramolecular dynamics on the sample environment. We performed a series of incoherent elastic neutron-scattering experiments on lyophilized human butyrylcholinesterase (HuBChE) powders under different conditions (solvent composition and hydration degree) in the temperature range from 20 to 285 K to elucidate the effect of the environment on the enzyme atomic mean-square displacements. Comparing D(2)O- with H(2)O-hydrated samples, we were able to investigate protein as well as hydration water molecular dynamics. HuBChE lyophilized from three distinct buffers showed completely different atomic mean-square displacements at temperatures above approximately 200 K: a salt-free sample and a sample containing Tris-HCl showed identical small-amplitude motions. A third sample, containing sodium phosphate, displayed highly reduced mean-square displacements at ambient temperature with respect to the other two samples. Below 200 K, all samples displayed similar mean-square displacements. We draw the conclusion that the reduction of intramolecular protein mean-square displacements on an Angstrom-nanosecond scale by the solvent depends not only on the presence of salt ions but also on their type.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-10963663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-11026689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-11053145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-11088920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-11104759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-11734642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12124295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12192064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12202382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12444262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12621860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12869558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12885619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-12944299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-13726518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-1463484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-1749823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-1986743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-2207247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-2918910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3179317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3255382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3293595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3542989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3843705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3916340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-3978078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-5928504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-7819239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-8089839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-8136015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-8176737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-8415760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9178088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9200697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9221822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9748494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9748500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15111428-9916036
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3152-65
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15111428-Biophysical Phenomena,
pubmed-meshheading:15111428-Biophysics,
pubmed-meshheading:15111428-Buffers,
pubmed-meshheading:15111428-Butyrylcholinesterase,
pubmed-meshheading:15111428-Deuterium Oxide,
pubmed-meshheading:15111428-Freeze Drying,
pubmed-meshheading:15111428-Humans,
pubmed-meshheading:15111428-Ions,
pubmed-meshheading:15111428-Models, Statistical,
pubmed-meshheading:15111428-Neutrons,
pubmed-meshheading:15111428-Protons,
pubmed-meshheading:15111428-Salts,
pubmed-meshheading:15111428-Scattering, Radiation,
pubmed-meshheading:15111428-Solvents,
pubmed-meshheading:15111428-Temperature,
pubmed-meshheading:15111428-Water
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pubmed:year |
2004
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pubmed:articleTitle |
The influence of solvent composition on global dynamics of human butyrylcholinesterase powders: a neutron-scattering study.
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pubmed:affiliation |
Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, Grenoble, France.
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