Individual amino acids in the N-terminal loop region determine the thermostability and unfolding characteristics of bacterial glucanases

Protein Science

Volumn 5, Issue 11, 1996, Pages 2255-2265

  Welfle, Karin ^a,b   Misselwitz, Rolf ^a,b   Politz, Oliver ^a,c   Borriss, Rainer ^a   Welfle, Heinz ^a,b  

^a HUMBOLDT UNIVERSITY   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^c CARLSBERG LABORATORY   (Denmark)

Author keywords

Bacillus amyloliquefaciens; Bacillus macerans; circular dichroism; conformation; differential scanning calorimetry; hybrid enzymes; stability, unfolding; glucanase

Indexed keywords

GLUCAN GLUCOSIDASE; HYBRID PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMOSTABILITY;

BACILLUS AMYLOLIQUEFACIENS; BACTERIA (MICROORGANISMS); MYCOBACTERIUM AVIUM COMPLEX (MAC); PAENIBACILLUS MACERANS;

EID: 0029825448     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051112     Document Type: Article

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