Bioengineering seminar: "Dynamic Allosteric Response in Protein Complexes - The role of hydrogen bonded water networks"
Event details
| Date | 15.09.2022 |
| Hour | 14:00 › 15:00 |
| Speaker | Professor Scott Prosser, University of Toronto Distinguished Professor of Biophysical Chemistry |
| Location | |
| Category | Conferences - Seminars |
| Event Language | English |
Abstract:
Protein folding is generally regarded as being driven by “hydrophobic collapse” – as the ribosome releases the nascent protein, secondary structure is rapidly acquired while tertiary structure is derived through the formation of van der Waals interactions between hydrophobic side chains and the simultaneous liberation of water molecules. Yet, in the final analysis, salt links and internal hydrogen bonds contribute nearly as much to the free energy of folding as hydrophobic forces. A key player in these hydrogen bonds is water and buried water molecules in hydrophobic interiors have the possibility of contributing to fold stability while also facilitating allostery and functional dynamics. Beginning with high-resolution crystal structures and computational analysis we consider water-mediated allostery in a dimeric enzyme, fluoroacetate dehalogenase, and a 7-transmembrane receptor, adenosine A2A. In both cases, we find networks of water molecules in hydrophobic environments. Computational studies, NMR, and functional assays reveal their dynamic role in assisting in functional dynamics and facilitating action of the protein in response to ligands and substrates.
Bio:
Professor Scott Prosser
Protein folding is generally regarded as being driven by “hydrophobic collapse” – as the ribosome releases the nascent protein, secondary structure is rapidly acquired while tertiary structure is derived through the formation of van der Waals interactions between hydrophobic side chains and the simultaneous liberation of water molecules. Yet, in the final analysis, salt links and internal hydrogen bonds contribute nearly as much to the free energy of folding as hydrophobic forces. A key player in these hydrogen bonds is water and buried water molecules in hydrophobic interiors have the possibility of contributing to fold stability while also facilitating allostery and functional dynamics. Beginning with high-resolution crystal structures and computational analysis we consider water-mediated allostery in a dimeric enzyme, fluoroacetate dehalogenase, and a 7-transmembrane receptor, adenosine A2A. In both cases, we find networks of water molecules in hydrophobic environments. Computational studies, NMR, and functional assays reveal their dynamic role in assisting in functional dynamics and facilitating action of the protein in response to ligands and substrates.
Bio:
Professor Scott Prosser
Professor of Chemistry and Biochemistry, University of Toronto since 2000
Assistant Professor of Chemistry, Kent State University
Postdoc, University of California, R Vold
Postdoc, University of Stuttgart G Kothe
PhD University of Guelph
Research focus - 19F NMR, GPCRs and signal transduction, enzymology, functional dynamics and allostery, drug screening, and biophysical chemistry of GPCRs
2017 Royal Society of Chemistry Jeremy Knowles Award for Advances in Chemical Biology
2019 University of Toronto Professor in Biophysical Chemistry
2022 Canadian Society for Chemistry. Biological and Medicinal Chemistry Lectureship Award
2022 AstraZeneca Endowed Chair in Biotechnology, University of Toronto.
2019 University of Toronto Professor in Biophysical Chemistry
2022 Canadian Society for Chemistry. Biological and Medicinal Chemistry Lectureship Award
2022 AstraZeneca Endowed Chair in Biotechnology, University of Toronto.
Practical information
- Informed public
- Free