The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase

Journal of Bacteriology

Volumn 187, Issue 17, 2005, Pages 6197-6205

  Siddiqui, Khawar S ^a   Feller, Georges ^b   D'Amico, Salvino ^b   Gerday, Charles ^b   Giaquinto, Laura ^a   Cavicchioli, Ricardo ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; AMYLASE INHIBITOR; CALCIUM ION; MUTANT PROTEIN; TROMETAMOL; UREA;

ARTICLE; COLD ACCLIMATIZATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; GEL ELECTROPHORESIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PSEUDOALTEROMONAS; PSEUDOALTEROMONAS HALOPLANKTIS; TEMPERATURE; TRANSVERSE UREA GRADIENT GEL ELECTROPHORESIS;

ALPHA-AMYLASE; ANTARCTIC REGIONS; BINDING SITES; COLD; ENZYME STABILITY; MODELS, MOLECULAR; MUTAGENESIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PSEUDOALTEROMONAS; RECOMBINATION, GENETIC;

BACTERIA (MICROORGANISMS); PSEUDOALTEROMONAS HALOPLANKTIS;

EID: 24344486447     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.17.6197-6205.2005     Document Type: Article

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