Homology modeling reveals the structural background of the striking difference in thermal stability between two related [NiFe]hydrogenases

Journal of Molecular Modeling

Volumn 8, Issue 2, 2002, Pages 58-64

  Szilágyi, András ^a,b   Kovács, Kornél L ^a,c   Rákhely, Gábor ^a,c   Závodszky, Péter ^a,b  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^c UNIVERSITY OF SZEGED   (Hungary)

Author keywords

Homology modeling; Hydrogenase; Mettalloenzymes; Protein stability; Thiocapsa roseopersicina

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; HYDROGEN; HYDROGENASE; IRON; NICKEL; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; COMPUTER PROGRAM; CONTROLLED STUDY; ELECTRICITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBUNIT; HYDROGEN BOND; MOLECULAR MODEL; NONHUMAN; POLARIZATION; PREDICTION; PRIORITY JOURNAL; PROTON TRANSPORT; RELIABILITY; SEQUENCE HOMOLOGY; SULFUR BACTERIUM; SURFACE PROPERTY; THERMOSTABILITY; THIOCAPSA ROSEOPERSICINA;

AMINO ACIDS; ELECTROSTATICS; ENZYME STABILITY; HYDROGENASE; MODELS, MOLECULAR; PROTEIN SUBUNITS; REPRODUCIBILITY OF RESULTS; STRUCTURAL HOMOLOGY, PROTEIN; TEMPERATURE; THIOCAPSA ROSEOPERSICINA;

BACTERIA (MICROORGANISMS); THIOCAPSA ROSEOPERSICINA;

EID: 0347928815     PISSN: 16102940     EISSN: None     Source Type: Journal    
DOI: 10.1007/S00894-001-0071-8     Document Type: Article

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