Structural basis of increased resistance to thermal denaturation induced by single amino acid substitution in the sequence of β-glucosidase a from Bacillus polymyxa

Proteins: Structure, Function and Genetics

Volumn 33, Issue 4, 1998, Pages 567-576

  Sanz Aparicio, J ^a   Hermoso, J A ^a   Martinez Ripoll M ^a   Gonzalez B ^a   Lopez Camacho C ^b   Polaina, J ^b  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b INSTITUTO DE AGROQUÍMICA Y TECNOLOGÍA DE ALIMENTOS CSIC   (Spain)

Author keywords

Bacterial cellobiase; Family 1; Mutated glucosidase; Thermoresistance; X ray structure

Indexed keywords

BETA GLUCOSIDASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; GENETIC ENGINEERING; NONHUMAN; PAENIBACILLUS POLYMYXA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; BACILLUS; BASE SEQUENCE; BETA-GLUCOSIDASE; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); PAENIBACILLUS POLYMYXA; POLYMYXA;

EID: 0032400469     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981201)33:4<567::AID-PROT9>3.0.CO;2-U     Document Type: Article

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