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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1992-5-6
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pubmed:abstractText |
The prediction of the folded structure of a protein from its sequence has proven to be a very difficult computational problem. We have developed an exceptionally simple representation of a polypeptide chain, with which we can enumerate all possible backbone conformations of small proteins. A protein is represented by a self-avoiding path of connected vertices on a tetrahedral lattice, with several amino acid residues assigned to each lattice vertex. For five small structurally dissimilar proteins, we find that we can separate native-like structures from the vast majority of non-native folds by using only simple structural and energetic criteria. This method demonstrates significant generality and predictive power without requiring foreknowledge of any native structural details.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-1094916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-1118010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-1153006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-1167625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-13683522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-17840193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2334692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2459709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2584229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2622905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2695928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2845278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-2845279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-3471114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-3477791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-4124164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-4351801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-5971783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-6317443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-6347038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-7327267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-7411610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-875032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-934293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-957439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1557356-978745
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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 |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2536-40
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1557356-Amino Acid Sequence,
pubmed-meshheading:1557356-Animals,
pubmed-meshheading:1557356-Cattle,
pubmed-meshheading:1557356-DNA-Binding Proteins,
pubmed-meshheading:1557356-Models, Molecular,
pubmed-meshheading:1557356-Models, Theoretical,
pubmed-meshheading:1557356-Molecular Sequence Data,
pubmed-meshheading:1557356-Neurotoxins,
pubmed-meshheading:1557356-Protein Conformation,
pubmed-meshheading:1557356-Repressor Proteins,
pubmed-meshheading:1557356-Ribosomal Proteins,
pubmed-meshheading:1557356-Rubredoxins,
pubmed-meshheading:1557356-Thermodynamics,
pubmed-meshheading:1557356-Trypsin Inhibitors,
pubmed-meshheading:1557356-Viral Proteins,
pubmed-meshheading:1557356-Viral Regulatory and Accessory Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
A lattice model for protein structure prediction at low resolution.
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pubmed:affiliation |
Beckman Laboratories for Structural Biology, Department of Cell Biology, Stanford University School of Medicine, CA 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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