Comparison of the molten globule states of thermophilic and mesophilic α-amylases

Biophysical Chemistry

Volumn 122, Issue 1, 2006, Pages 58-65

  Shokri, Maryam Monsef ^a   Khajeh, Khosro ^a   Alikhajeh, Jahan ^a   Asoodeh, Ahmad ^a   Ranjbar, Bijan ^a   Hosseinkhani, Saman ^a   Sadeghi, Mehdi ^b  

^a TARBIAT MODARES UNIVERSITY   (Iran)

^b NATIONAL INSTITUTE OF GENETIC ENGINEERING AND BIOTECHNOLOGY   (Iran)

Author keywords

amylase; Aggregation; Folding pathway; Molten globule states; Stability

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLASE; BACTERIAL ENZYME; ENZYME; GLYCEROL; GUANIDINE; PEPSIN A; POLYOL; SORBITOL; TREHALOSE;

ARTICLE; BACILLUS LICHENIFORMIS; CIRCULAR DICHROISM; FLUORESCENCE; GEL FILTRATION; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ALPHA-AMYLASE; BACILLUS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN FOLDING; TIME FACTORS;

BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS;

EID: 33744972619     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.12.014     Document Type: Article

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