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rdf:type |
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lifeskim:mentions |
umls-concept:C0012634,
umls-concept:C0041942,
umls-concept:C0205409,
umls-concept:C0332120,
umls-concept:C0598629,
umls-concept:C1442792,
umls-concept:C1514562,
umls-concept:C1704332,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
4
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pubmed:dateCreated |
1999-7-14
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pubmed:abstractText |
The objective of this study was to evaluate the suitability of the WW domain as a desirable model system to understand the folding and stability of an isolated three-stranded antiparallel beta-sheet structure. The WW domain was subjected to thermal and chaotropic denaturation/reconstitution utilizing a variety of biophysical methods. This three-stranded sheet folds reversibly and cooperatively utilizing both urea and GdnHCl as denaturants; however, the denatured state retains structure in the form of a hydrophobic cluster involving at least one aromatic side chain. In contrast to chaotropic denaturation, thermal denaturation appears to be more complete and may be a two state process. The suitability of the WW domain for future studies aimed at understanding the kinetics and thermodynamics of antiparallel beta-sheet folding clearly emerges from this initial study. The most exciting and significant result in this manuscript is the finding that the chaotropic denatured state of WW has a hydrophobic cluster as discerned by near-UV CD evidence. The role that the denatured state plays in the folding and stability of a three-stranded beta-sheets, and its capacity for preventing aggregation may be particularly important and is the subject of ongoing studies.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-1390650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-1390769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-1523410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-1867725,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-1883209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-2110472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-2449095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-3233195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-3663854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-3773761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-4066779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-4680720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7508991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7613459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7632873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7644498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7664054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7703845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7805627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-7846762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8035999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8078589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8086409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8107853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8180173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8241116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8298454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8519746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8566543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8639594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8696966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8757138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-8818225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9029943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9200606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9202023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9224934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9283083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9356142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9519302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9521124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9593201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10211830-9657719
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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 |
Apr
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10211830-Humans,
pubmed-meshheading:10211830-Urea,
pubmed-meshheading:10211830-Temperature,
pubmed-meshheading:10211830-Thermodynamics,
pubmed-meshheading:10211830-Guanidine,
pubmed-meshheading:10211830-Kinetics,
pubmed-meshheading:10211830-Biochemical Phenomena,
pubmed-meshheading:10211830-Protein Binding,
pubmed-meshheading:10211830-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10211830-Protein Denaturation,
pubmed-meshheading:10211830-Dose-Response Relationship, Drug,
pubmed-meshheading:10211830-Models, Statistical,
pubmed-meshheading:10211830-Circular Dichroism,
pubmed-meshheading:10211830-Spectrometry, Fluorescence,
pubmed-meshheading:10211830-Carrier Proteins,
pubmed-meshheading:10211830-Protein Structure, Secondary,
pubmed-meshheading:10211830-Protein Structure, Tertiary,
pubmed-meshheading:10211830-Phosphoproteins,
pubmed-meshheading:10211830-Protein Folding
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