The link between structure and function of a given protein is a principal tenet of biology. The established approach to understand the function of a protein is to ‘solve’ its structure and subsequently investigate interactions between the protein and its binding partners. However, structure determination via crystallography or NMR is challenging for proteins where localized regions or even their entire structure fail to fold into a three-dimensional form. These so called IDPs (intrinsically disordered proteins) or intrinsically disordered regions constitute up to 40% of all expressed proteins, and a much higher percentage in proteins involved in the proliferation of cancer. For these proteins, there is a need to develop new methods for structural characterization which exploit their biophysical properties. IM (ion mobility)–MS is uniquely able to examine both absolute conformation(s), populations of conformation and also conformational change, and is therefore highly applicable to the study of IDPs. The present article details the technique of IM–MS and illustrates its use in assessing the relative disorder of the wild-type p53 DNA-core-binding domain of cellular tumour antigen p53. The IM data were acquired on a Waters Synapt HDMS instrument following nESI (nanoelectrospray ionization) from ‘native’ and low-pH solution conditions.
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October 2012
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Conference Article|
September 19 2012
Intrinsic disorder in proteins: a challenge for (un)structural biology met by ion mobility–mass spectrometry
Ewa Jurneczko;
Ewa Jurneczko
*EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, West Mains Road, Edinburgh EH9 3JJ, U.K.
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Faye Cruickshank;
Faye Cruickshank
*EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, West Mains Road, Edinburgh EH9 3JJ, U.K.
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Massimiliano Porrini;
Massimiliano Porrini
*EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, West Mains Road, Edinburgh EH9 3JJ, U.K.
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Penka Nikolova;
Penka Nikolova
†School of Biomedical Sciences, Kings College London, Hodgkin Building, Guy's Campus, London SE1 1UL, U.K.
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Iain D.G. Campuzano;
Iain D.G. Campuzano
1
‡Waters Corporation, Floats Road, Wythenshawe, Manchester M23 9LZ, U.K.
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Michael Morris;
Michael Morris
‡Waters Corporation, Floats Road, Wythenshawe, Manchester M23 9LZ, U.K.
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Perdita E. Barran
Perdita E. Barran
2
*EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, West Mains Road, Edinburgh EH9 3JJ, U.K.
2To whom correspondence should be addressed (emailperdita.barran@ed.ac.uk).
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Publisher: Portland Press Ltd
Received:
May 01 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem Soc Trans (2012) 40 (5): 1021–1026.
Article history
Received:
May 01 2012
Citation
Ewa Jurneczko, Faye Cruickshank, Massimiliano Porrini, Penka Nikolova, Iain D.G. Campuzano, Michael Morris, Perdita E. Barran; Intrinsic disorder in proteins: a challenge for (un)structural biology met by ion mobility–mass spectrometry. Biochem Soc Trans 1 October 2012; 40 (5): 1021–1026. doi: https://doi.org/10.1042/BST20120125
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