Number of the records: 1  

Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin

  1. 1.
    SYSNO ASEP0327972
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleAnalysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin
    Author(s) Berka, Karel (UOCHB-X)
    Hobza, Pavel (UOCHB-X) RID, ORCID
    Vondrášek, Jiří (UOCHB-X) RID, ORCID
    Number of authors3
    Source TitleChemPhysChem. - : Wiley - ISSN 1439-4235
    Roč. 10, č. 3 (2009), s. 543-548
    Number of pages6 s.
    Languageeng - English
    CountryDE - Germany
    Keywordshydrophobic core ; protein stability ; SAPT method
    Subject RIVCF - Physical ; Theoretical Chemistry
    R&D ProjectsGA203/05/0009 GA ČR - Czech Science Foundation (CSF)
    GA203/06/1727 GA ČR - Czech Science Foundation (CSF)
    GD203/05/H001 GA ČR - Czech Science Foundation (CSF)
    IAA400550510 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    LC512 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    CEZAV0Z40550506 - UOCHB-X (2005-2011)
    UT WOS000264229900014
    DOI10.1002/cphc.200800401
    AnnotationThe hydrophobic core of globular proteins is responsible for major stabilization of the protein tertiary structure. The prevailing amino-acid residues in the core are of aliphatic or aromatic character, and therefore, the core in a folded protein structure is mostly stabilized by noncovalent interactions of van der Waals origin between the amino-acid side chains. Herein, we present a theoretical analysis of the interaction energy between the amino acids of the hydrophobic core of the small globular protein rubredoxin (Rd) based on the symmetry-adapted perturbation theory (SAPT) method.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    Contactasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
    Year of Publishing2010
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.