Colloids Seminar: Dr Eamonn Reading
Dr Eamonn Reading
Dr Eamonn Reading (King's College London)
"Exploring the role of lipids in shaping membrane protein structure, dynamics, and folding"
Cell membranes are highly complex and dynamic organizations of lipids and membrane proteins responsible for many specialized cellular functions. Lipids are amphipathic small molecules which can self-assemble into lipid bilayers, in an aqueous environment, and form the basis of biological membranes. Membrane proteins reside within these lipid bilayers. Membrane protein-lipid interplay is important for cellular function, however, tools enabling the interrogation of membrane protein structure, dynamics and folding, in the context of their lipid environment, are scarce and often invasive.
We have developed methods capable of investigating membrane proteins within the context of their lipid partners. Namely, ion mobility native mass spectrometry (IM-MS), hydrogen-deuterium exchange MS (HDX-MS), and surface enhanced infrared spectroscopy (SEIRAS). Utilization of these techniques enabled novel insights into membrane protein conformational dynamics, co-translational folding, and lipid binding to be obtained.
The potential for these emerging techniques in examining membrane proteins, in well-defined lipid environments, is an exciting prospect which we anticipate will impact on the membrane protein structural biology field, as well as on drug discovery pipelines.
- Structure formation during translocon-unassisted co-translational membrane protein folding, Sci. Rep., 7, 8021. (2017)
- The effect of detergent, temperature and lipid on the oligomeric state of MscL constructs: Insights from mass spectrometry, Chem. Biol., 22, 593-603. (2015)
- Membrane proteins bind lipids selectively to modulate their structure and function, Nature, 510, 172-175. (2014)
Dr Wuge Briscoe
School of Chemistry
Ph: 0117 331 8256