High solubility supports efficient refolding of thermally unfolded β-lactamase

International Journal of Biological Macromolecules

Volumn 47, Issue 5, 2010, Pages 706-709

  Arakawa, Tsutomu ^a   Tokunaga, Hiroko ^b   Yamaguchi, Rui ^b   Tokunaga, Masao ^b  

^a ALLIANCE PROTEIN LABORATORIES   (United States)

^b KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

Aggregation; Beta lactamase; Refolding; Reversibility; Unfolding

Indexed keywords

BETA LACTAMASE; HALOPHILIC BETA LACTAMASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG; UREA;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; MELTING POINT; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; ROOM TEMPERATURE; SALINITY; SOLUBILITY; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS; THERMOSTABILITY;

EID: 77958174651     PISSN: 01418130     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2010.09.009     Document Type: Article

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