The mutations Lys 114 → Gln and Asp 126 → Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps. Effects on protein stability at low pH

Proteins: Structure, Function and Genetics

Volumn 66, Issue 4, 2007, Pages 975-983

  Bellapadrona, Giuliano ^a   Chiaraluce, Roberta ^a   Consalvi, Valerio ^a   Ilari, Andrea ^a   Stefanini, Simonetta ^a   Chiancone, Emilia ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

L. innocua Dps; L. monocytogenes Dps; Multimeric proteins; pH stability; X ray crystallography

Indexed keywords

AMINO ACID; ASPARAGINE; ASPARTIC ACID; BACTERIAL PROTEIN; GLUTAMINE; LYSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENERGY; GENE MUTATION; HIGH TEMPERATURE; HYDROGEN BOND; KINETICS; LISTERIA MONOCYTOGENES; MOLECULAR INTERACTION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS; ULTRAVIOLET SPECTROSCOPY; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; BACTERIAL PROTEINS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; HYDROGEN-ION CONCENTRATION; KINETICS; LISTERIA; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SALTS; SOLUTIONS; TEMPERATURE;

LISTERIA INNOCUA; LISTERIA MONOCYTOGENES;

EID: 33847067891     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21305     Document Type: Article

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