The early career academics presenting in the next Peptide and Protein Science online series will be Manuel M眉ller from the King鈥檚 College and Fabio Parmeggiani from the Bristol University.
Manuel M眉ller 鈥� King鈥檚 College
Title: Probing Life and Death Decisions with Protein Semisynthesis
Post-translational modifications (PTMs) of proteins control almost all biological processes, including cellular life and death decisions. Such processes serve to eliminate aberrant cells and are mediated by endogenous proteins - including the tumour suppressor p53 - and can be hijacked by pathogen-encoded toxic proteins. Deciphering how PTMs regulate the activity of these 鈥渟elf-destruction鈥� proteins is an important step in understanding the basic biology of controlled cell death and in providing a framework for the design of new antitumour proteins. However, mechanistic analysis of how PTMs effect structural and functional changes is hampered by the complexity of the underlying signalling pathways and thus requires chemistry-driven approaches which we develop. I will discuss our protein semisynthesis strategies to access 鈥渄esigner p53鈥� and a viral anticancer protein bearing defined PTMs, and how we are deploying these proteins in functional assays in vitro and in living cells to gain new insights into how PTMs decide cell fate.
Fabio Parmeggiani 鈥� Bristol University
Title: Designed repeat proteins: longer, faster and more creative
Repeat proteins have seen a progressive rise in interest as scaffolds for novel binders or as parts of large protein architectures.
In my group, we exploit the intrinsic modularity of repeat proteins to develop computational and experimental methods to design and produce novel structures. I will describe our software tools for designing proteins from modular units (Elfin/ElfinUI), our work on DNA assemblies of repetitive units and the design of novel interfaces for formation of repeat protein complexes.
Our goal is to simplify and speed up design of complex protein architectures to be used as scaffolds for novel functional nanomaterials and nanoparticles.
For upcoming series, please visit the RSC PPSG website
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: louise.walport@crick.ac.uk
Manuel M眉ller 鈥� King鈥檚 College
Title: Probing Life and Death Decisions with Protein Semisynthesis
Post-translational modifications (PTMs) of proteins control almost all biological processes, including cellular life and death decisions. Such processes serve to eliminate aberrant cells and are mediated by endogenous proteins - including the tumour suppressor p53 - and can be hijacked by pathogen-encoded toxic proteins. Deciphering how PTMs regulate the activity of these 鈥渟elf-destruction鈥� proteins is an important step in understanding the basic biology of controlled cell death and in providing a framework for the design of new antitumour proteins. However, mechanistic analysis of how PTMs effect structural and functional changes is hampered by the complexity of the underlying signalling pathways and thus requires chemistry-driven approaches which we develop. I will discuss our protein semisynthesis strategies to access 鈥渄esigner p53鈥� and a viral anticancer protein bearing defined PTMs, and how we are deploying these proteins in functional assays in vitro and in living cells to gain new insights into how PTMs decide cell fate.
Fabio Parmeggiani 鈥� Bristol University
Title: Designed repeat proteins: longer, faster and more creative
Repeat proteins have seen a progressive rise in interest as scaffolds for novel binders or as parts of large protein architectures.
In my group, we exploit the intrinsic modularity of repeat proteins to develop computational and experimental methods to design and produce novel structures. I will describe our software tools for designing proteins from modular units (Elfin/ElfinUI), our work on DNA assemblies of repetitive units and the design of novel interfaces for formation of repeat protein complexes.
Our goal is to simplify and speed up design of complex protein architectures to be used as scaffolds for novel functional nanomaterials and nanoparticles.
For upcoming series, please visit the RSC PPSG website
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: louise.walport@crick.ac.uk
