Experimental and computational characterization of the dimerization of the PTS-regulation domains of BglG from Escherichia coli

Journal of Molecular Biology

Volumn 347, Issue 4, 2005, Pages 693-706

  Ben Zeev, Efrat ^a   Fux, Liat ^b   Amster Choder, Orna ^b   Eisenstein, Miriam ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

Electrostatic desolvation energy; Geometric electrostatic docking; Protein recognition; Regulation of BglG; Transcription antitermination

Indexed keywords

BACTERIAL PROTEIN; DIMER; HISTIDINE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN BGLG; PROTEIN LICT; UNCLASSIFIED DRUG;

ARTICLE; COMPUTER ANALYSIS; COMPUTER MODEL; COMPUTER PROGRAM; CONTROLLED STUDY; DIMERIZATION; ELECTRICITY; ESCHERICHIA COLI; EXPERIMENT; GEOMETRY; IN VIVO STUDY; MUTATION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; SCORING SYSTEM;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 14844358499     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.068     Document Type: Article

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