Insights into the Conformations of Three Structurally Diverse Proteins: Cytochrome c, p53, and MDM2, Provided by Variable-Temperature Ion Mobility Mass Spectrometry

Analytical Chemistry

Volumn 87, Issue 6, 2015, Pages 3231-3238

  Dickinson, Eleanor R ^a   Jurneczko, Ewa ^b   Pacholarz, Kamila J ^a   Clarke, David J ^b   Reeves, Matthew ^b   Ball, Kathryn L ^b   Hupp, Ted ^b   Campopiano, Dominic ^b   Nikolova, Penka V ^c   Barran, Perdita E ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

^c KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

COMPACTION; DIMERS; ION MOBILITY SPECTROMETERS; IONS; MASS SPECTROMETRY; PROTEINS; SPECTROMETRY;

COLLISION CROSS SECTIONS; CONFORMATIONAL TRANSITIONS; ION MOBILITY-MASS SPECTROMETRY; ION-MOBILITY MEASUREMENTS; MULTIPLE CONFORMATIONS; NATIVE MASS SPECTROMETRIES; STRUCTURAL REARRANGEMENT; TUMOR SUPPRESSOR PROTEINS;

CONFORMATIONS;

CYTOCHROME C; DNA; PROTEIN MDM2; PROTEIN P53;

ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; MASS SPECTROMETRY; METABOLISM; PROCEDURES; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

ANIMALS; CYTOCHROMES C; DNA; MASS SPECTROMETRY; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MDM2; TEMPERATURE; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84924974987     PISSN: 00032700     EISSN: 15206882     Source Type: Journal    
DOI: 10.1021/ac503720v     Document Type: Article

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