Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel

Protein Engineering

Volumn 10, Issue 12, 1997, Pages 1433-1443

  Cheley, Stephen ^a   Malghani, M S ^b   Song, Langzhou ^c   Hobaugh, Michael ^c   Gouaux, J Eric ^c   Yang, Jie ^b   Bayley, Hagan ^a  

^a TEXAS A AND M HEALTH SCIENCE CENTER   (United States)

^b University of Vermont   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

hemolysin; toxin; Channel; Pore; Transmembrane barrel

Indexed keywords

HEMOLYSIN; MEMBRANE PROTEIN; MUTANT PROTEIN; STAPHYLOCOCCUS TOXIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; HEMOLYSIS; MEMBRANE CHANNEL; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL TOXINS; BASE SEQUENCE; ENDOPEPTIDASE K; ERYTHROCYTE MEMBRANE; GLYCINE; HEMOLYSIN PROTEINS; HEMOLYSIS; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RABBITS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0031404458     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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