Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 42, Issue -, Pages 167-176Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2017.12.013
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/L009501/1, BB/M012557/1, BB/R000182/1]
- Biotechnology and Biological Sciences Research Council (BBSRC) (BBSRC DTP studentship)
- North West Cancer Research [CR1037, CR1088]
- Institute of Integrative Biology, University of Liverpool
- BBSRC [BB/R000182/1, BB/L009501/1, BB/M012557/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L009501/1, BB/M012557/1, BB/R000182/1] Funding Source: researchfish
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Ion mobility-mass spectrometry (IM-MS) is an important addition to the analytical toolbox for the structural evaluation of proteins, and is enhancing many areas of biophysical analysis. Disease-associated proteins, including enzymes such as protein kinases, transcription factors exemplified by p53, and intrinsically disordered proteins, including those prone to aggregation, are all amenable to structural analysis by IM-MS. In this review we discuss how this powerful technique can be used to understand protein conformational dynamics and aggregation pathways, and in particular, the effect that small molecules, including clinically-relevant drugs, play in these processes. We also present examples of how IM-MS can be used as a relatively rapid screening strategy to evaluate the mechanisms and conformation-driven aspects of protein:ligand interactions.
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