Functional and structural interactions of the transmembrane domain X of NhaA, Na+/H+ antiporter of Escherichia coli, at physiological pH

Biochemistry

Volumn 46, Issue 9, 2007, Pages 2419-2430

  Kozachkov, Lena ^a   Herz, Katia ^a   Padan, Etana ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORT; CYSTEINE-SCANNING MUTAGENESIS; STRUCTURAL-BASED EVOLUTIONARY APPROACH;

CONFORMATIONS; MOLECULAR STRUCTURE; MUTAGENESIS; PH EFFECTS; PHYSIOLOGY; SILICA;

ESCHERICHIA COLI;

2 SULFONATOETHYL METHANETHIOSULFONATE; CYSTEINE; GLYCINE; LITHIUM ION; LYSINE; N ETHYLMALEIMIDE; PROTEIN NHAA; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; COMPUTER MODEL; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; ESCHERICHIA COLI; EVOLUTION; MOLECULAR INTERACTION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; REGULATORY MECHANISM;

BASE SEQUENCE; CYSTEINE; DNA PRIMERS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PROTEIN CONFORMATION; SODIUM-HYDROGEN ANTIPORTER;

ESCHERICHIA COLI;

EID: 33847650845     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602393s     Document Type: Article

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