Source:http://linkedlifedata.com/resource/pubmed/id/17151953
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-12-28
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pubmed:abstractText |
Chemical shifts contain substantial information about protein local conformations. We present a method to assign individual protein backbone dihedral angles into specific regions on the Ramachandran map based on the amino acid sequences and the chemical shifts of backbone atoms of tripeptide segments. The method uses a scoring function derived from the Bayesian probability for the central residue of a query tripeptide segment to have a particular conformation. The Ramachandran map is partitioned into representative regions at two levels of resolution. The lower resolution partitioning is equivalent to the conventional definitions of different secondary structure regions on the map. At the higher resolution level, the alpha and beta regions are further divided into subregions. Predictions are attempted at both levels of resolution. We compared our method with TALOS using the original TALOS database, and obtained comparable results. Although TALOS may produce the best results with currently available databases which are much enlarged, the Bayesian-probability-based approach can provide a quantitative measure for the reliability of predictions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0925-2738
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31-41
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pubmed:meshHeading |
pubmed-meshheading:17151953-Algorithms,
pubmed-meshheading:17151953-Bayes Theorem,
pubmed-meshheading:17151953-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17151953-Probability,
pubmed-meshheading:17151953-Protein Conformation,
pubmed-meshheading:17151953-Proteins,
pubmed-meshheading:17151953-Reproducibility of Results
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pubmed:year |
2007
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pubmed:articleTitle |
A Bayesian-probability-based method for assigning protein backbone dihedral angles based on chemical shifts and local sequences.
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pubmed:affiliation |
Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230027, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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