Articles producció científica> Bioquímica i Biotecnologia

SRide: a server for identifying stabilizing residues in proteins

  • Dades identificatives

    Identificador: imarina:5116649
    Autors:
    Magyar, CGromiha, MMPujadas, GTusnady, GESimon, I
    Resum:
    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.
  • Altres:

    Autor segons l'article: Magyar, C; Gromiha, MM; Pujadas, G; Tusnady, GE; Simon, I;
    Departament: Bioquímica i Biotecnologia
    e-ISSN: 1362-4962
    Autor/s de la URV: Pujadas Anguiano, Gerard
    Paraules clau: Long-range interactions Identification Folded proteins Centers
    Resum: 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.
    Àrees temàtiques: 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
    Accès a la llicència d'ús: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 0305-1048
    Adreça de correu electrònic de l'autor: gerard.pujadas@urv.cat
    Identificador de l'autor: 0000-0003-2598-8089
    Pàgina final: W305
    Data d'alta del registre: 2023-02-18
    Volum de revista: 33
    Versió de l'article dipositat: info:eu-repo/semantics/publishedVersion
    Referència a l'article segons font original: Nucleic Acids Research. 33 (Supl 2): W303-W305
    Referència 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 Document de llicència: https://repositori.urv.cat/ca/proteccio-de-dades/
    Entitat: Universitat Rovira i Virgili
    Any de publicació de la revista: 2005
    Pàgina inicial: W303
    Tipus de publicació: Journal Publications
  • Paraules clau:

    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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