Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Web Server issue
pubmed:dateCreated
2007-7-16
pubmed:abstractText
The side chains of the 20 types of amino acids, owing to a large extent to their different physical properties, have characteristic distributions in interior/surface regions of individual proteins and in interface/non-interface portions of protein surfaces that bind proteins or nucleic acids. These distributions have important structural and functional implications. We have developed accurate methods for predicting the solvent accessibility of amino acids from a protein sequence and for predicting interface residues from the structure of a protein-binding or DNA-binding protein. The methods are called WESA, cons-PPISP and DISPLAR, respectively. The web servers of these methods are now available at http://pipe.scs.fsu.edu. To illustrate the utility of these web servers, cons-PPISP and DISPLAR predictions are used to construct a structural model for a multicomponent protein-DNA complex.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-11402327, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-11455607, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-12784371, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-15613384, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-15906321, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-15937195, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-15980475, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-15981252, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16080151, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16427316, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16568445, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16641487, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16672257, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16712732, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16793544, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16809388, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16845003, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16893954, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-16919296, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-17284455, http://linkedlifedata.com/resource/pubmed/commentcorrection/17526530-9254694
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1362-4962
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
W357-62
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
PI2PE: protein interface/interior prediction engine.
pubmed:affiliation
Institute of Molecular Biophysics and School of Computational Science and Department of Physics, Florida State University, Tallahassee, FL 32306, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural