Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53

Journal of the American Chemical Society

Volumn 134, Issue 3, 2012, Pages 1617-1622

  Lum, Jenifer K ^a   Neuweiler, Hannes ^a,b   Fersht, Alan R ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PARTNERS; CHAIN MOTIONS; CONFORMATIONAL ENSEMBLE; DISORDERED DOMAINS; FLUORESCENCE CORRELATION SPECTROSCOPY; FLUORESCENCE QUENCHING; HUB PROTEINS; LOCAL STRUCTURE; LONG RANGE INTERACTIONS; LOOP CLOSURE; N-TERMINAL DOMAINS; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN BINDING; RANDOM COIL; REMOTE REGIONS; TRANSACTIVATION DOMAIN; TUMOR SUPPRESSORS;

AMINO ACIDS; BIOCHEMISTRY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; KINETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHORYLATION; PROTEINS;

TUMORS;

PROTEIN MDM2; PROTEIN P53; TRYPTOPHAN;

ALLOSTERISM; ARTICLE; BINDING KINETICS; FLUORESCENCE; FLUORESCENCE CORRELATION SPECTROSCOPY; KINETICS; MODULATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN SYNTHESIS; TRANSACTIVATION;

AMINO ACID SEQUENCE; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MDM2; SPECTROMETRY, FLUORESCENCE; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84856303585     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja2078619     Document Type: Article

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