The unwound portion dividing helix iv of nhaa undergoes a conformational change at physiological pH and lines the cation passage

Biochemistry

Volumn 51, Issue 47, 2012, Pages 9560-9569

  Rimon, Abraham ^a   Kozachkov Magrisso, Lena ^a   Padan, Etana ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTERS; APPARENT K; CONFORMATIONAL CHANGE; CONSERVED RESIDUES; CYS REPLACEMENT; E. COLI; HIGH-PRESSURE MEMBRANES; INTACT CELLS; METHANETHIOSULFONATE; OUTER MEMBRANE; PERMEABLE BARRIER; PH REGULATION; PH VALUE; PHYSIOLOGICAL PH; POSITIVELY CHARGED; TRANSMEMBRANE SEGMENTS;

BROMINE COMPOUNDS; ESCHERICHIA COLI; PH EFFECTS;

PHYSIOLOGY;

2 SULFONATOETHYL METHANETHIOSULFONATE; [2 (TRIMETHYLAMMONIUM)ETHYL]METHANETHIOSULFONATE BROMIDE; BROMINE DERIVATIVE; CATION; CYSTEINE; PROTEIN NHAA; SODIUM PROTON EXCHANGE PROTEIN; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL OUTER MEMBRANE; CELL MEMBRANE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ESCHERICHIA COLI; MICHAELIS CONSTANT; NONHUMAN; PERMEABILITY BARRIER; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; CATIONS; CELL MEMBRANE PERMEABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MESYLATES; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; SODIUM-HYDROGEN ANTIPORTER;

ESCHERICHIA COLI;

EID: 84870195905     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301030x     Document Type: Article

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