Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition

FEBS Letters

Volumn 580, Issue 11, 2006, Pages 2646-2652

  Sivakumar, Neelamegam ^a   Li, Nan ^a   Tang, Julian W ^a   Patel, Bharat K C ^c   Swaminathan, Kunchithapadam ^a,b  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c Faculty of Environmental Sciences   (Australia)

Author keywords

Amylase; Halophilic; Oligomerization; Poly extreme; Thermophilic

Indexed keywords

AMYLASE; OLIGOMER;

ACIDITY; ANAEROBIC BACTERIUM; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; HALOPHILIC BACTERIUM; HALOTHERMOTHRIX ORENII; HIGH TEMPERATURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; SALINITY; SEDIMENTATION RATE; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

ACIDS; ALPHA-AMYLASE; BINDING SITES; CALCIUM; CIRCULAR DICHROISM; CLOSTRIDIUM; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

BACTERIA (MICROORGANISMS); HALOTHERMOTHRIX ORENII;

EID: 33646205656     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.04.017     Document Type: Article

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