Structural requirements of the unique disulphide bond and the proline-rich motif within the α4-α5 loop for larvicidal activity of the Bacillus thuringiensis Cry4Aa δ-endotoxin

Biochemical and Biophysical Research Communications

Volumn 330, Issue 2, 2005, Pages 519-525

  Tapaneeyakorn, Satita ^a   Pornwiroon, Walairat ^a   Katzenmeier, Gerd ^a   Angsuthanasombat, Chanan ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Bacillus thuringiensis; Disulphide bond; Larvicidal activity; Mutagenesis; Proline rich motif; Endotoxin

Indexed keywords

BACILLUS THURINGIENSIS TOXIN; CARBONIC ACID; ENDOTOXIN; MEMBRANE PROTEIN; MUTANT PROTEIN; PROLINE; PROTOXIN; TRYPSIN;

AEDES AEGYPTI; ARTICLE; BACILLUS THURINGIENSIS; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE MUTATION; LARVA; MUTAGENESIS; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILIZATION; WILD TYPE;

EID: 15744376728     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.03.006     Document Type: Article

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