Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state

Biochemistry

Volumn 52, Issue 20, 2013, Pages 3457-3463

  Vargas Uribe, Mauricio ^a   Rodnin, Mykola V ^a   Kienker, Paul ^b   Finkelstein, Alan ^b   Ladokhin, Alexey S ^a  

^a UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM MEASUREMENTS; CONDUCTANCE MEASUREMENT; CONFORMATIONAL CHANGE; DIPHTHERIA TOXIN; MEMBRANE FOLDING; MEMBRANE INSERTION; SPECTROSCOPIC SIGNATURES; TRYPTOPHAN FLUORESCENCE;

ACIDIFICATION; AMINO ACIDS; LIPID BILAYERS;

MEMBRANES;

DIPHTHERIA TOXIN; GLUTAMINE; HISTIDINE; HISTIDINE H322; LYSINE; MUTANT PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ACIDIFICATION; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CIRCULAR DICHROISM; FLUORESCENCE; GENE INSERTION; LOSS OF FUNCTION MUTATION; MEMBRANE BIOLOGY; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROSCOPY; WILD TYPE;

BINDING SITES; CIRCULAR DICHROISM; DIPHTHERIA TOXIN; HISTIDINE; HYDROGEN-ION CONCENTRATION; LIPID BILAYERS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; TRYPTOPHAN;

EID: 84878229869     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400249f     Document Type: Article

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