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Volumn 29, Issue 4, 2001, Pages 571-577

Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms

(4) Li, J a Derbyshire, D J a Promdonkoy, B a Ellar, D J a

a MRC LABORATORY OF MOLECULAR BIOLOGY (United Kingdom)

Author keywords

Conformational change; Metastable; Model membranes; Mutagenesis; Receptor binding

Indexed keywords

ENDOTOXIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; BACILLUS THURINGIENSIS; BINDING SITE; CELL SURFACE; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; GENE MUTATION; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; RECEPTOR BINDING; STRUCTURE ANALYSIS;

BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BACTERIAL TOXINS; ENDOTOXINS; HEMOLYSIN PROTEINS; MODELS, MOLECULAR; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SOLUBILITY;

BACILLUS THURINGIENSIS; INSECTA;

EID: 0034859678 PISSN: 03005127 EISSN: None Source Type: Journal
DOI: 10.1042/BST0290571 Document Type: Conference Paper

Times cited : (61)

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