Solvent-exposed residues in the Tet repressor (TetR) four-helix bundle contribute to subunit recognition and dimer stability

Journal of Biological Chemistry

Volumn 274, Issue 10, 1999, Pages 6405-6410

  Schnappinger, Dirk ^a   Schubert, Peter ^a   Berens, Christian ^a   Pfleiderer, Klaus ^a   Hillen, Wolfgang ^a  

^a UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; DIMER; GLUTAMIC ACID; MONOMER; PROTEIN SUBUNIT; REPRESSOR PROTEIN; SOLVENT;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; DIMERIZATION; HYDROPHOBICITY; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN STABILITY; REPRESSOR GENE;

AMINO ACID SEQUENCE; DIMERIZATION; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; REPRESSOR PROTEINS; SEQUENCE DELETION;

EID: 0033525890     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.10.6405     Document Type: Article

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