STING Contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces.
Bioinformatics
; 20(13): 2145-7, 2004 Sep 01.
Article
en En
| MEDLINE
| ID: mdl-15073001
UNLABELLED: Amino acid contacts in terms of atomic interactions are essential factors to be considered in the analysis of the structure of a protein and its complexes. Consequently, molecular biologists do require specific tools for the identification and visualization of all such contacts. Graphical contacts (GC) and interface forming residue graphical contacts (IFRgc) presented here, calculate atomic contacts among amino acids based on a table of predefined pairs of the atom types and their distances, and then display them using number of different forms. The inventory of currently listed contact types by GC and IFRgc include hydrogen bonds (in nine different flavors), hydrophobic interactions, charge-charge interactions, aromatic stacking and disulfide bonds. Such extensive catalog of the interactions, representing the forces that govern protein folding, stability and binding, is the key feature of these two applications. GC and IFRgc are part of STING Millennium Suite. AVAILABILITY: http://sms.cbi.cnptia.embrapa.br/SMS, http://trantor.bioc.columbia.edu/SMS, http://mirrors.rcsb.org//SMS, http://www.es.embnet.org/SMS and http://www.ar.embnet.org/SMS (Options: Graphical Contacts and IFR Graphical Contacts).
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Algoritmos
/
Proteínas
/
Modelos Moleculares
/
Internet
/
Mapeo de Interacción de Proteínas
/
Aminoácidos
/
Modelos Químicos
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Idioma:
En
Revista:
Bioinformatics
Asunto de la revista:
INFORMATICA MEDICA
Año:
2004
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Reino Unido