Dr Jennifer McManus
The Chemical and Physical Factors Directing the Self-assembly of Proteins
The ability to control the self-assembly of biological molecules to form defined or functional structures with a high degree of predictability is a central aim for soft matter science and synthetic biology. While this is possible for a variety of colloidal materials, it has been more difficult to achieve for proteins. In large part, this is due to the complex chemical nature of the protein surface, which influences the assembly process. It is therefore important to understand this complexity to reveal the mechanisms underlying important processes such as protein crystallization, the pathogenesis of protein condensation diseases, the aggregation of proteins during industrial manufacture and the formation of protein based materials. Recent results probing the extent to which protein surface anisotropic interactions influence protein self-assembly will be presented. Using phase diagrams for human gamma D-crystallin (a protein found in the human eye lens), both mutagenesis and chemical modification of the protein surface are used to probe the effect of altering the protein anisotropy at the molecular level - demonstrating that relatively minor changes to the protein surface can dramatically alter its phase behaviour.
ABOUT THE PRESENTER
Dr Jennifer McManus is a senior lecturer in chemistry at Maynooth University. She received her B.Sc. and Ph.D. degrees in Chemistry from University College Dublin and after a period of postdoctoral research at the University of Fribourg in Switzerland and the Massachusetts Institute of Technology in the department of Physics (Benedek Group), established the Soft Matter and Biophysical Chemistry research group at Maynooth University as a Science Foundation Ireland Stokes Lecturer. Her current research focus is the self-assembly of proteins. Her research group explores protein phase transitions and in particular how protein surface chemistry drives the assembly process and the mechanisms leading to protein aggregation.
DATE: Thursday, 9 February 2017
VENUE: MSG-025 MSSI Building Extension
TEA/COFFEE WILL BE AVAILABLE AT 11h45
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