Assembly of a transmembrane b-Type cytochrome is mainly driven by transmembrane helix interactions

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 11, 2006, Pages 1815-1822

  Volkmer, Thomas ^a   Becker, Christian ^b   Prodöhl, Alexander ^a   Finger, Carmen ^a   Schneider, Dirk ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Assembly; Cytochrome; Heme; Membrane protein folding; Two stage model

Indexed keywords

AMINO ACID; CYTOCHROME B; DETERGENT; FLUORESCENT DYE; HEME; MEMBRANE PROTEIN; MONOMER;

ARTICLE; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; MEASUREMENT; MICELLE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY;

AMINO ACID SEQUENCE; BINDING SITES; CELL MEMBRANE; COENZYMES; CYTOCHROME B GROUP; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; HEME; MEMBRANE PROTEINS; MICELLES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PHOTOSYSTEM II PROTEIN COMPLEX; PROTEIN FOLDING;

EID: 33750509171     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.05.009     Document Type: Article

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