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Angewandte Chemie - International Edition

Volumn 52, Issue 1, 2013, Pages 361-365

Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase

(5) Pagel, Kevin a,c Natan, Eviatar b Hall, Zoe a Fersht, Alan R b Robinson, Carol V a

a UNIVERSITY OF OXFORD (United Kingdom)

b MRC LABORATORY OF MOLECULAR BIOLOGY (United Kingdom)

c FRITZ HABER INSTITUT DER MAX PLANCK GESELLSCHAFT (Germany)

Author keywords

Analytical methods; Disordered proteins; Ion mobility; Mass spectrometry; Protein folding

Indexed keywords

ANALYTICAL METHOD; DISORDERED PROTEINS; GASPHASE; ION MOBILITY; ION MOBILITY-MASS SPECTROMETRY; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN SEQUENCES; SUB-DOMAINS; TUMOR SUPPRESSOR PROTEINS;

CONFORMATIONS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; PROTEIN FOLDING; PROTEINS;

GASES;

PROTEIN P53;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GAS; HUMAN; MASS SPECTROMETRY; METABOLISM; MOLECULAR DYNAMICS; PROTEIN FOLDING;

GASES; HUMANS; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN FOLDING; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84871981207 PISSN: 14337851 EISSN: 15213773 Source Type: Journal
DOI: 10.1002/anie.201203047 Document Type: Article

Times cited : (78)

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