Articles producció científica> Bioquímica i Biotecnologia

SRide: a server for identifying stabilizing residues in proteins

  • Datos identificativos

    Identificador: imarina:5116649
    Autores:
    Magyar, CGromiha, MMPujadas, GTusnady, GESimon, I
    Resumen:
    Residues expected to play key roles in the stabilization of proteins [stabilizing residues (SRs)] are selected by combining several methods based mainly on the interactions of a given residue with its spatial, rather than its sequential neighborhood and by considering the evolutionary conservation of the residues. A residue is selected as a stabilizing residue if it has high surrounding hydrophobicity, high long-range order, high conservation score and if it belongs to a stabilization center. The definition of all these parameters and the thresholds used to identify the SRs are discussed in detail. The algorithm for identifying SRs was originally developed for TIM-barrel proteins [M. M. Gromiha, G. Pujadas, C. Magyar, S. Selvaraj, and I. Simon (2004), Proteins, 55, 316-329] and is now generalized for all proteins of known 3D structure. SRs could be applied in protein engineering and homology modeling and could also help to explain certain folds with significant stability. The SRide server is located at http://sride.enzim.hu.
  • Otros:

    Autor según el artículo: Magyar, C; Gromiha, MM; Pujadas, G; Tusnady, GE; Simon, I;
    Departamento: Bioquímica i Biotecnologia
    e-ISSN: 1362-4962
    Autor/es de la URV: Pujadas Anguiano, Gerard
    Palabras clave: Long-range interactions Identification Folded proteins Centers
    Resumen: Residues expected to play key roles in the stabilization of proteins [stabilizing residues (SRs)] are selected by combining several methods based mainly on the interactions of a given residue with its spatial, rather than its sequential neighborhood and by considering the evolutionary conservation of the residues. A residue is selected as a stabilizing residue if it has high surrounding hydrophobicity, high long-range order, high conservation score and if it belongs to a stabilization center. The definition of all these parameters and the thresholds used to identify the SRs are discussed in detail. The algorithm for identifying SRs was originally developed for TIM-barrel proteins [M. M. Gromiha, G. Pujadas, C. Magyar, S. Selvaraj, and I. Simon (2004), Proteins, 55, 316-329] and is now generalized for all proteins of known 3D structure. SRs could be applied in protein engineering and homology modeling and could also help to explain certain folds with significant stability. The SRide server is located at http://sride.enzim.hu.
    Áreas temáticas: Zootecnia / recursos pesqueiros Saúde coletiva Química Nutrição Medicina ii Medicina i Matemática / probabilidade e estatística Interdisciplinar Genetics Farmacia Engenharias ii Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Ciências agrárias i Ciência da computação Biotecnología Biodiversidade Biochemistry & molecular biology Astronomia / física
    Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 0305-1048
    Direcció de correo del autor: gerard.pujadas@urv.cat
    Identificador del autor: 0000-0003-2598-8089
    Página final: W305
    Fecha de alta del registro: 2023-02-18
    Volumen de revista: 33
    Versión del articulo depositado: info:eu-repo/semantics/publishedVersion
    Enlace a la fuente original: https://academic.oup.com/nar/article/33/suppl_2/W303/2505549
    Referencia al articulo segun fuente origial: Nucleic Acids Research. 33 (Supl 2): W303-W305
    Referencia de l'ítem segons les normes APA: Magyar, C; Gromiha, MM; Pujadas, G; Tusnady, GE; Simon, I; (2005). SRide: a server for identifying stabilizing residues in proteins. Nucleic Acids Research, 33(Supl 2), W303-W305. DOI: 10.1093/nar/gki409
    URL Documento de licencia: https://repositori.urv.cat/ca/proteccio-de-dades/
    DOI del artículo: 10.1093/nar/gki409
    Entidad: Universitat Rovira i Virgili
    Año de publicación de la revista: 2005
    Página inicial: W303
    Tipo de publicación: Journal Publications
  • Palabras clave:

    Biochemistry & Molecular Biology,Genetics
    Long-range interactions
    Identification
    Folded proteins
    Centers
    Zootecnia / recursos pesqueiros
    Saúde coletiva
    Química
    Nutrição
    Medicina ii
    Medicina i
    Matemática / probabilidade e estatística
    Interdisciplinar
    Genetics
    Farmacia
    Engenharias ii
    Ciências biológicas iii
    Ciências biológicas ii
    Ciências biológicas i
    Ciências agrárias i
    Ciência da computação
    Biotecnología
    Biodiversidade
    Biochemistry & molecular biology
    Astronomia / física
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