Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na +/H + antiporter NhaA

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 38, 2011, Pages 15769-15774

  Kozachkov, Lena ^a   Padan, Etana ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

Membrane proteins; Secondary transporters; Transporter functional dynamics

Indexed keywords

NHAA PROTEIN; SODIUM PROTON EXCHANGE PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALKALINITY; ARTICLE; BACTERIAL MUTATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENTEROBACTERIACEAE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HOMEOSTASIS; HUMAN; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STRUCTURE ACTIVITY RELATION;

AMINO ACID SUBSTITUTION; CELL MEMBRANE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; LITHIUM; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; SODIUM; SODIUM-HYDROGEN ANTIPORTER; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ENTEROBACTERIACEAE; ESCHERICHIA COLI; HOMO SAPIENS;

EID: 80053162595     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1109256108     Document Type: Article

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