Lectures and Events - Faculty of Chemistry

Upcoming Lectures

  • February25

    11:00 AM

    Dolfi and Lola Ebner Auditorium

    "Augmenting biology through de novo protein design"

    Prof. Dek Woolfson

    Protein design—i.e., the construction of entirely new protein sequences that fold into prescribed structures—has come...

    Protein design—i.e., the construction of entirely new protein sequences that fold into prescribed structures—has come of age: it is possible now to generate a wide variety stable protein folds from scratch using rational and/or computational approaches. A challenge for the field is to move from what have been largely in vitro exercises to protein design in living cells and, in so doing, to augment biology. This talk will illustrate what is currently possible in this nascent field using de novo -helical coiled-coil peptides as building blocks.1 Coiled coils are bundles of 2 or more  helices that wrap around each other to form rope-like structures. They are one of the dominant structures that direct natural protein-protein interactions. Our understanding of coiled coils provides a strong basis for building new proteins from the bottom up. The first part of this talk will survey this understanding,1 our design methods,2,3 and our current “toolkit” of de novo coiled coils.4-6 Next, I will describe how the toolkit can be used to direct protein-protein interactions and build complex protein assemblies in bacterial cells. First, in collaboration with the Savery lab (Bristol), we have used homo- and hetero-oligomeric coiled coils as modules in engineered and de novo transcriptional activators and repressors.7 Secondly, with the Warren (Kent) and the Verkade (Bristol) labs, we have engineered hybrids of a de novo heterodimer and a natural component of bacterial microcompartments to form a “cytoscaffold” that permeates E. coli cells.8 This can be used to support the co-localisation of functional enzymes.

  • March11

    11:00 AM

    Max and Lillian Candiotty Building

    "Supramolecular Assembly with Mechanical Action"

    Prof. Myongsoo Lee

    In this symposium, I will introduce our recent results how to construct dynamic self-assembled nanostructures...

    In this symposium, I will introduce our recent results how to construct dynamic self-assembled nanostructures exhibiting switchable functions, inspired by life systems. For example, synthetic tubular pores are able to undergo open-closed gating driven by an external signal, which function as an artificial enzyme. When self-assembled tubules embed DNA inside the hollow cavities, the DNA-coat assembly undergoes collective motion in helicity switching. In the case of toroid assembly, the static toroids are able to undergo spontaneous helical growth when they switch into out-of-equilibrium state. The helical growing drives actuation of spherical vesicles into tubular vesicles, reminiscent of microtubles. Moving from 1-D to 2-D structures, the internal pores are able to form chiral interior which selectively capture only one enantiomer in racemic solution with pumping action. I will discuss recently discovered these results with their complex functions.

  • March18

    11:00 AM

    Max and Lillian Candiotty Building

    Chemistry colloquium

    Prof. Lei Jiang

  • April15

    11:00 AM

    Max and Lillian Candiotty Building

    Chemistry Colloquium

    Prof. Jan Schroers

  • October23

    08:00 AM

    David Lopatie Conference Centre

    Contemporary Crystal Engineering and Solid-State Chemistry: Symposium commemorating G. M. J. Schmidt's 100th birthday anniversary

  • April05

    08:00 AM

    David Lopatie Conference Centre

    Kimmel Auditorium

    Soft matter (tentative)