Articles producció científica> Bioquímica i Biotecnologia

SRide: a server for identifying stabilizing residues in proteins

  • Identification data

    Identifier: imarina:5116649
    Authors:
    Magyar, CGromiha, MMPujadas, GTusnady, GESimon, I
    Abstract:
    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.
  • Others:

    Author, as appears in the article.: Magyar, C; Gromiha, MM; Pujadas, G; Tusnady, GE; Simon, I;
    Department: Bioquímica i Biotecnologia
    e-ISSN: 1362-4962
    URV's Author/s: Pujadas Anguiano, Gerard
    Keywords: Long-range interactions Identification Folded proteins Centers
    Abstract: 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.
    Thematic Areas: 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
    licence for use: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 0305-1048
    Author's mail: gerard.pujadas@urv.cat
    Author identifier: 0000-0003-2598-8089
    Last page: W305
    Record's date: 2023-02-18
    Journal volume: 33
    Papper version: info:eu-repo/semantics/publishedVersion
    Link to the original source: https://academic.oup.com/nar/article/33/suppl_2/W303/2505549
    Papper original source: Nucleic Acids Research. 33 (Supl 2): W303-W305
    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
    Licence document URL: https://repositori.urv.cat/ca/proteccio-de-dades/
    Article's DOI: 10.1093/nar/gki409
    Entity: Universitat Rovira i Virgili
    Journal publication year: 2005
    First page: W303
    Publication Type: Journal Publications
  • Keywords:

    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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