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Bioscience Research Group Seminar Series

Here are the full details of The University of Hertfordshire's Bioscience Research Group seminars, sponsored by the Biochemical Society.

Our next seminar will take place on 20 January 2021

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Learn about our past events

  • Not covering up with skin: a route to birth defects? 9 December 2020

    Delivered by Dr Caroline Formstone, Department of Clinical, Pharmaceutical & Biological Science, University of Hertfordshire, UK

    The skin provides a protective layer for the body against desiccation and external assault. How skin is built in the embryo has been long studied but little is known about how it encompasses the body. My research has shown that the skin emerges in mouse embryos just over half-way through gestation. The skin appears as a thickened tissue at the mid-flank of the embryo trunk which subsequently thins and spreads from the mid-flank towards the front of the embryo (ventral-side) and the back of the embryo (dorsal-side) eventually enclosing the embryo trunk 2-3 days later. I will provide evidence that skin enclosure of the embryo body requires both intrinsic and extrinsic processes. Overall, my research raises the hypothesis that failure to enclose the embryo body with skin may underlie some common birth defects of dorsal and ventral closure and importantly that extrinsic factors may reduce their prevalence.

  • Dynamic interaction networks and conformational plasticity of the SARS-CoV-2 protein S - 11 November 2020

    Delivered by Prof. Ana-Nicoleta Bondar, Department of Physics, Freie Universität Berlin, Germany

    The new SARS-CoV-2 virus is known to bind via the spike protein (protein S) to the human host ACE2 receptor followed by proteolytic activation of S. Structural signatures of conformations sampled by protein S were identified with graph-based algorithms in static structures and simulations of protein S. We found that the closed conformation of protein S has, at key functional sites, three-fold symmetrical H-bond clusters. Loss of three-fold symmetry as observed in open and closed conformations of the spike protein could facilitate conformational selection for receptor and protease interactions. Instead of discrete interaction pairs, the receptor-binding interface consists of an extensive interaction network that includes multiple groups from both protein S and ACE2, which could explain strong binding affinity and provide robustness.

  • Protein dynamics in signalling and in multi-enzyme complexes - 14 October 2020

    Delivered by Dr. Bill Broadhurst, Department of Biochemistry, University of Cambridge

    I will provide a brief introduction to protein dynamics on different timescales and ways of quantifying these processes, with a particular focus on NMR spectroscopy. I will then discuss an application to the conformational plasticity of ligand-bound ternary complexes of the beta1-adrenergic receptor, a model G-protein coupled receptor (Nature Communications (2020) 11, 669). After that I will describe some of my work on the dynamics of acyl carrier protein domains in modular polyketide synthase multienzyme complexes (Biochemical J (2016) 473, 1097-1110; Scientific Reports (2019) 9, 2325; Chemical Comm (2017) 53, 11457-11460).