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Volumn 76, Issue 3, 2009, Pages 548-559

Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli

Author keywords

Conformation; Continuum electrostatics; NhaA Na + H + antiporter; pH dependent activation; Single mutations

Indexed keywords

ANTIPORTER; GLUTAMIC ACID; SODIUM PROTON ANTIPORTER NHAA; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 68049148763     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22368     Document Type: Article
Times cited : (23)

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