Tandem Mass Spectrometry Defines the Stoichiometry and Quaternary Structural Arrangement of Tryptophan Molecules in the Multiprotein Complex TRAP

Journal of the American Chemical Society

Volumn 126, Issue 19, 2004, Pages 5950-5951

  McCammon, Margaret G ^a   Hernández, Helena ^a   Sobott, Frank ^a   Robinson, Carol V ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MONOMER; OLIGOMER; PROTEIN; RNA BINDING PROTEIN; TRYPTOPHAN; TRYPTOPHAN RNA BINDING ATTENUATION PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; ARTICLE; COLLISIONALLY ACTIVATED DISSOCIATION; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STOICHIOMETRY; TANDEM MASS SPECTROMETRY;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BUFFERS; CRYSTALLOGRAPHY, X-RAY; MASS SPECTROMETRY; RNA-BINDING PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TRANSCRIPTION FACTORS; TRYPTOPHAN;

EID: 2442527851     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0317170     Document Type: Article

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