The internal cavity of the staphylococcal α-hemolysin pore accommodates ∼175 exogenous amino acid residues

Biochemistry

Volumn 44, Issue 25, 2005, Pages 8919-8929

  Jung, Yuni ^a   Cheley, Stephen ^a   Braha, Orit ^b   Bayley, Hagan ^b  

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

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ELECTROPHORESIS; ENZYMES; LIPIDS; POLYPEPTIDES;

Α-HEMOLYSIN; ELECTROPHORETIC MIGRATION; HOMOMERIC PORES; LIPID BILAYERS;

BACTERIA;

ALPHA HEMOLYSIN; GLYCINE; HEMOLYSIN; PROTEIN SUBUNIT; SERINE; STAPHYLOCOCCUS TOXIN; UNCLASSIFIED DRUG;

ARTICLE; CHANNEL GATING; DNA SEQUENCE; GENE INSERTION SEQUENCE; GENE MUTATION; LIPID BILAYER; MEMBRANE CONDUCTANCE; MEMBRANE CURRENT; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; WILD TYPE;

AMINO ACIDS; BACTERIAL TOXINS; BASE SEQUENCE; DNA, BACTERIAL; GLYCINE; HEMOLYSIN PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SERINE; STAPHYLOCOCCUS; TEMPERATURE;

EID: 21744440132     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0473713     Document Type: Article

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