|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0052872,
umls-concept:C0185026,
umls-concept:C0678257,
umls-concept:C0678594,
umls-concept:C0679083,
umls-concept:C0681814,
umls-concept:C1442792,
umls-concept:C1609982,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C1880022
|
|
pubmed:issue |
25
|
|
pubmed:dateCreated |
1998-1-15
|
|
pubmed:abstractText |
Residual structure in the denatured state of a protein may contain clues about the early events in folding. We have simulated by molecular dynamics the denatured state of barnase, which has been studied by NMR spectroscopy. An ensemble of 10(4) structures was generated after 2 ns of unfolding and following for a further 2 ns. The ensemble was heterogeneous, but there was nonrandom, residual structure with persistent interactions. Helical structure in the C-terminal portion of helix alpha1 (residues 13-17) and in helix alpha2 as well as a turn and nonnative hydrophobic clustering between beta3 and beta4 were observed, consistent with NMR data. In addition, there were tertiary contacts between residues in alpha1 and the C-terminal portion of the beta-sheet. The simulated structures allow the rudimentary NMR data to be fleshed out. The consistency between simulation and experiment inspires confidence in the methods. A description of the folding pathway of barnase from the denatured to the native state can be constructed by combining the simulation with experimental data from phi value analysis and NMR.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1523410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1569556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1569558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1569559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1786342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-1888730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-2018757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-2739734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-5722263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7490750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7508991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7563082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7577994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7626612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7756310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7756312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7773750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7932708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-7937780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8142379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8513892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8519746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8580852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8609634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8683584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8696969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8855224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-8880914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9032066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9079363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9079384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9092826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9149150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9200680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391038-9220986
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
9
|
|
pubmed:volume |
94
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
13409-13
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:9391038-Amino Acid Sequence,
pubmed-meshheading:9391038-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9391038-Models, Molecular,
pubmed-meshheading:9391038-Molecular Sequence Data,
pubmed-meshheading:9391038-Protein Denaturation,
pubmed-meshheading:9391038-Protein Folding,
pubmed-meshheading:9391038-Protein Structure, Secondary,
pubmed-meshheading:9391038-Ribonucleases,
pubmed-meshheading:9391038-Static Electricity,
pubmed-meshheading:9391038-Temperature,
pubmed-meshheading:9391038-Thermodynamics
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway.
|
|
pubmed:affiliation |
Department of Medicinal Chemistry, University of Washington, Seattle, WA 98195-7610, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|
