Intrinsic disorder in proteins: A challenge for (un)structural biology met by ion mobility-mass spectrometry

Biochemical Society Transactions

Volumn 40, Issue 5, 2012, Pages 1021-1026

  Jurneczko, Ewa ^a   Cruickshank, Faye ^a   Porrini, Massimiliano ^a   Nikolova, Penka ^b   Campuzano, Iain D G ^c,d   Morris, Michael ^c   Barran, Perdita E ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

^c WATERS CORPORATION   (United States)

^d AMGEN INC   (United States)

Author keywords

Intrinsically disordered protein; Ion mobility mass spectrometry; p53

Indexed keywords

ARGININE; INTRINSICALLY DISORDERED PROTEIN; LYSINE; PROTEIN; PROTEIN P53; UNCLASSIFIED DRUG; ZINC;

ASYMMETRIC WAVEFORM ION MOBILITY SPECTROMETRY; BINDING SITE; BIOLOGY; CELL PROLIFERATION; DNA BINDING; DNA DAMAGE; ELECTROSPRAY MASS SPECTROMETRY; ION MOBILITY SPECTROMETRY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING; PROTON TRANSPORT; REVIEW; SPECTROMETRY;

HYDROGEN-ION CONCENTRATION; MASS SPECTROMETRY; PROTEIN CONFORMATION; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84866713162     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120125     Document Type: Review

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