The UCL Faculties of Engineering, Mathematical & Physical Sciences and Life Sciences will lead seven new government-funded Centres for Doctoral Training and be a partner in a further two.
EPSRC has agreed to provide funding for a new Centre for Doctoral Training in Accelerated Medicines Design & Development (AMD&D) (~£7M) with the first student intake scheduled for autumn 2025.
Our CDT will recruit over 50 PhD students to develop the advanced laboratory and computational skills needed to accelerate medicines design and overcome the major obstacles in medicines development. The CDT is a partnership between UCL, the University of Nottingham, and a network of industrial and clinical partners from across the UK pharmaceutical, healthcare and medical technologies sector.
Prof Gareth Williams is the UCL CDT Director and will run the CDT together with UCL Co-Directors Prof Simon Gaisford, Prof Helen Hailes, Professor Rio Torii, Professor Jonathan Knowles and colleagues from Nottingham who are CoIs on the grant.
Read the article on UCL website here.
The Engineering Biology Mission Hubs aim to harness cutting-edge engineering biology research from across the UK to address global challenges from health to the environment. The six hubs will receive up to £12 million each from the UKRI Technology Missions Fund and the Biotechnology and Biological Sciences Research Council (BBSRC).
The P3EB Mission Hub (funded with £12.3M) aims to tackle the urgent environmental challenge of plastic pollution and create new ways for the sustainable deconstruction of synthetic plastics as the UK transitions towards a circular plastics economy. The hub will be led by Professor Andrew Pickford (University of Portsmouth), with support from scientists from seven leading UK institutions, including UCL co-investigators: Professor Helen Hailes (UCL Chemistry), Dr Jack Jeffries (UCL Biochemical Engineering), Professor Mark Miodownik (UCL Mechanical Engineering), Professor Paola Lettieri (UCL Chemical Engineering), Dr Andrea Paulillo (UCL Chemical Engineering), Dr Brooks Paige (UCL Centre for Artificial Intelligence), Professor Christine Orengo (UCL Biosciences).
Read the story here.
Dive into the intriguing world of technological trust with us at the Science Museum’s thought-provoking event, “Can We Trust Computers?”. Join us on Thursday, 9 May 2024, from 18:30 to 19:30, at the IMAX: The Ronson Theatre, for a captivating panel discussion featuring leading experts like Dr. Alessandra Vizzaccaro and Professors Paul Brenner, Tim Palmer, and Peter Coveney, chaired by BBC broadcaster and journalist, Timandra Harkness.
We tackle pressing questions surrounding AI, computer reliability, and the complexities of digital versus analogue worlds. Is it prudent to entrust nuclear weapons to AI? This event promises a deep exploration into these vital questions, framed by real-world implications and expert insights.
Tickets are just £5, and doors open at 18:00. Reserve your spot now for an evening of engaging dialogue on the future of our trust in computers.
For more details and to book your tickets, please visit the Science Museum’s event page: Can We Trust Computers?.
A bid team which included UCL’s Professor Konstantinos Thalassinos has secured £49.35m from the UKRI Infrastructure Fund to establish a nationwide mass spectrometry infrastructure.
Critical Mass UK (C-MASS) will be a national hub-and-spoke infrastructure that will integrate and advance the UK’s capability in mass spectrometry, a technique that identifies the characteristics of molecules.
Mass spectrometry is used across a wide range of scientific research and C-MASS will enable large-scale screening and accelerated data access and sharing.
It will bring together cutting-edge instrumentation at a range of laboratories connected by a coordinating central hub that will manage a central metadata catalogue.
This will enable researchers to enhance their understanding of new materials required for quantum technologies, semiconductors, batteries, catalysts, medicines and more.
C-MASS will also be a critical health resource for the UK, for example by allowing researchers to combine datasets leading to key information about respiratory health from patients’ blood which can be compared with data on air quality.
Professor Konstantinos Thalassinos, academic lead of the UCL Mass Spectrometry Science Technology Platform, said: “I am thrilled by the funding secured for this groundbreaking mass spectrometry infrastructure. This investment will equip numerous labs across the UK with state-of-the-art mass spectrometers, fostering a collaborative approach to tackle significant challenges that are beyond the reach of any single lab.
“A cornerstone of this initiative is the establishment of a comprehensive data hub. This hub will not only coordinate activities but also crucially store data and metadata.
“The availability of such a resource will not only enable us to gain unprecedented insights from the data but will also be instrumental in advancing AI efforts. As we all know, these approaches heavily rely on large volumes of high-quality data, which the C-MASS data hub will provide. By harnessing the power of AI, we can unlock the full potential of this data, driving innovation and discovery in ways we can’t even imagine yet. This is a monumental step forward for scientific research in the UK, and I am thrilled to be part of this journey.”
The School of Natural Sciences at Birkbeck are delighted to invite you to this annual lecture in memory of Professor JD Bernal.
Established in 1968, this annual lecture commemorates JD Bernal – Professor of Physics at Birkbeck from 1938 and then Chair of Crystallography in 1963. In line with Bernal’s interests in structural biology, X-ray crystallography and, especially, the social consequences of science, this year we are pleased to welcome Professor Ravindra Gupta, Professor of Clinical Microbiology at the Cambridge Institute for Therapeutic Immunology and Infectious Diseases, University of Cambridge, for a talk titled “SARS CoV-2 : keeping up with an unprecedented pathogen“.
The SARS CoV-2 pandemic was unique in many ways, and the virus continues to surprise us with its ability to adapt and evolve. This is driven largely by an ability to persist in immune compromised individuals. In this talk we will explore how variants of concern arise and how we can stay ahead to prevent ongoing morbidity and mortality
This event is free to attend but booking is essential.
The prevalent state of DNA in all cells is chromatin that is made of protein-DNA complexes which are dynamic, complex and heterogenous. The exact composition of the chromatin determines its properties, how it regulates transcription and genome architecture. A breakthrough article by the RNAP laboratory at UCL published today in the journal Nature Communications describes how two chromatin proteins, Cbp1 and Cren7, collaborate to modulate gene regulation in opposing ways. While this type of specialised chromatin stimulates the expression of long crRNA arrays that facilitate adaptive immunity in archaea (‘CRISPR’), it cryptic promoters that frequently reside in the memory of the ‘immunity’ system, in the ‘CRISPR spacers’. This transcription interference by cryptic promoters limits how much spacer information can be stored in CRISPR arrays, or worse lead the malfunction of the system. Dr. Fabian Blombach from the ISMB RNAP laboratory, the lead author of the study, says ‘There is a lot of attention in the field to histones and their role in gene regulation, but we can learn so much from archaeal and bacterial chromatin proteins, including some of the ground rules that shape the interaction between chromatin proteins and transcription in all cellular life.’
Sulfolobus Cbp1 and Cren7 form chimeric chromatin structures on large archaeal CRISPR arrays. Cbp1 confers sequence-specificity and interacts via its HTH3 domain interactions with Cren7. Together, they enhance leader promoters but repress CRISPR spacer-encoded cryptic promoters1. Archaea research in the RNAP lab is funded by the Wellcome Trust Investigator in Science Award (WT207446/Z/17/Z).
References
Full paper can be read here.
Finn Werner’s group published a paper in Nature Communications on 22nd February.
The paper studies the mechanism of how viruses enter and replicate in the hosts cells is of fundamental importance to understand how they cause disease and developing tools for control.
A team of scientists at UCL, led by Prof Finn Werner, have taken a major step forward in understanding how African swine fever virus (ASFV) genes are controlled are expressed. ASFV causes a fatal disease of domestic pigs and wild boar that results in severe socio-economic impacts in affected countries in Africa Europe, Asia and parts of Oceana and the Caribbean. The lack of tools including vaccines or antivirals limits control of disease.
ASFV replicates in the host cell cytoplasm and uses its own machinery to transcribe its genes into mRNAs which are translated into proteins required for virus replication or modulating host cell function. The UCL team have expressed and assembled 8 proteins comprising the ASFV RNA polymerase into an active complex. The cryo-EM structure of this complex molecular machine was determined providing the information to further probe how it functions to regulate ASFV gene expression. Dr Pilotto says: ‘The production of recombinant eukaryotic RNA polymerases remains the bottleneck for structural studies and high-throughput inhibitor screenings. Our success with the ASFV RNAP represents a game-changer in the field’. The ASFV RNAP bears a striking resemblance to RNAPII – and key differences include the fusion of the ‘assembly platform subunits’ and an unusual fusion with a domain related to the eukaryotic mRNA capping enzyme. Together, the changes represent adaptions to streamline the enzyme to serve the virus best: allowing for efficient RNAP biogenesis, and mRNA expression and processing. The availability of a recombinant functional RNA polymerase will facilitate high throughput screening of antiviral compounds to identify compounds with sufficient specificity and selectivity.
This research will be further developed in a recently funded BBSRC collaborative research project between UCL and The Pirbright Institute (led by Drs Linda Dixon and Chris Netherton). This project will identify other accessory virus and host factors involved in regulating the temporal expression of ASFV genes and the packaging of the virus RNA polymerase into particles ready to start a next round of infection. This information is critical to understand the ASFV replication cycle and potential host factors that may limit virus replication.
Evolution and structure of ASFV RNAP. All DPBB RNAP share a common ancestry (A), the cryoEM structure of the 8-subunit ASFV RNAP (B), and model of the RNAP-capping enzyme complex showing the interaction with the CE (N7-MTase in orange, vRPB7 in blue/magenta) 1. ASFV research in the RNAP lab is funded by the BBSRC (BB/X015424/1) and Wellcome Trust (108877/B/15/Z).
Reference
Full paper can be read here.
Together with the Topf lab at the Centre for Structural Systems Biology (Hamburg), Kish Adoni from the Thalassinos lab has developed a novel pipeline that incorporates crosslinking-mass spectrometry data into AlphaFold2 for improved accuracy of protein structure determination. They found this workflow to be of particular relevance to proteins that occupy multiple conformations. The function of a protein is determined by its structure, via the structure-function relationship, and thousands of proteins modify their shape upon external cues such as molecular or protein interactions. As such, probing these conformational modifications is pivotal to characterising the protein’s behaviour, for example in the context of drug design when developing pharmaceuticals for drug-protein interactions.
Full paper can be read here.
Professor Helen Saibil’s research group published a paper titled ‘Structural basis of substrate progression through the bacterialchaperonin cycle’ in the PNAS Journal on 23 October 2023.
The full paper is available here.