Confirmed list of invited speakers:
Katrin Rittinger (The Francis Crick Institute, London)
Professor Dame Carol Robinson (Department of Chemistry, University of Oxford)
Riki Eggert (Randall Division of Cell and Molecular Biophysics, King’s College, London)
David Agard (Macromolecular Structure Group, University of California, San Francisco)
Richard Bayliss (The Astbury Centre for Structural Molecular Biology, University of Leeds)
Hagan Bayley (Department of Chemistry, University of Oxford)
John Briggs (MRC Laboratory of Molecular Biology, Cambridge)
Babis Kalodimos (Department of Structural Biology, St. Jude Children's Research Hospital)
Jim Naismith (Division of Structural Biology, University of Oxford) (Director of the Research Complex at Harwell)
Adam Nelson (The Astbury Centre for Structural Molecular Biology, University of Leeds)
Matthias Rief (The Institute of Molecular and Cellular Biophysics, Technical University of Munich)
Further talks will be selected from submitted abstracts.
Monday 16 and Tuesday 17 April 2018
Allostery in Biology
Join other researchers, academics and organisations in looking at the latest science. Network with people and learn about their specialisms and developments.
A packed programme will feature internationally-renowned speakers and researchers from closer to home, culminating in a lecture from Nobel Prize winner Professor Brian Kobilka.
|Monday 16th April|
|10:00||Arrival and registration: Parkinson Court|
|Session 1: The Great Hall (chair Tom Edwards, University of Leeds):|
|10:35||Welcome to the Astbury Conversation (Sheena Radford, Director of the Astbury Centre)|
|10:40||Introduction to the Astbury Conversation Symposium (Tom Edwards, Deputy Director of the Astbury Centre)|
|10:45||Richard Bayliss (University of Leeds): Dynamics and disorder in kinases and their binding partners|
|11:15||Elizabeth Morris (The Francis Crick Institute, London): Allostery and dynamics in cellular dNTP regulation by HIV-1 restriction factor SAMHD1|
|11:30||Lotte van Beek (University of York): Tandem domains go a long way: Repetitive domains form an elongated stalk in a biofilm-forming protein|
|11:45||Carol Robinson (University of Oxford): From peripheral proteins to membrane motors - mass spectrometry comes of age.|
|12:30 – 13:45||Lunch: Parkinson Court
|Session 2: The Great Hall (chair Jenn Potts, University of York):|
|13:45||David Agard (University of California, San Francisco): Protein Folding as an Allosteric Strategy: The Yin and Yang of Hsp90-mediated Client Activation|
|14:15||Anastasia Zhuravleva (University of Leeds): Conformational and functional flexibility of the molecular chaperone BiP|
|14:30||Lisa Jones (University of Maryland): Development of In-Cell and In Vivo Footprinting Coupled with Mass Spectrometry for the Structural Analysis of Proteins in their Native Environment|
|14:45||Jim Naismith (University of Oxford): Enzymatic manipulation of peptides: making what is hard look easy|
|15:30 – 16:00||Coffee Break: Parkinson Court
|Session 3: The Great Hall (chair Christina Redfield, University of Oxford):|
|16:00||Babis Kalodimos (University of Minnesota): Allosteric interactions in protein kinases|
|16:30||Anna Higgins (University of Leeds): Determining the mechanism of BAM-assisted OMP folding|
|16:45||Jeremy Tame (Yokohama City University): Photoactivation of a light-regulated adenylate cyclase|
|17:00||Katrin Rittinger (The Francis Crick Institute, London): Protein ubiquitination: there’s more than one way to get modified|
|17:30 – 18:00||Photo Session: Outside the Great Hall|
|18:00||Meet the editors panel discussion, Great Hall|
|18:30||Brian Kobilka (Stanford University): Structural insights into the dynamic process of G protein coupled receptor activation, Great Hall|
|19:00 until late||Posters with Pizza & beer: The Refectory
Poster session A 19:00 – 20:00, session B 20:00 – 21:00
|Tuesday 17th April|
|8:30||Arrival: Coffee Room UG09 (next to the Great Hall)|
|Session 4: The Great Hall (chair Madhulika Nambiar, Heptares TBC):|
|9:00||Paul Varley (Medimmune) Structural Biology and BioPharmaceutical Development|
|9:15||Zara Sands, UCB|
|9:30||Adam Nelson (University of Leeds): Nature-inspired approaches for bioactive small molecule discovery|
|10:00||Meni Wanunu (Northeastern University): Studying Biomolecules using Force and Temperature Control in Nanopores|
|10:15||Jeroen van Dyk (University of Antwerp): The activation and oligomerization of BAX after treatment with different activating compounds.|
|10:30 – 11:15||Coffee break (with exhibitors & CCPs): The Refectory|
|Session 5: The Great Hall (chair Travis Beddoe, La Trobe University):|
|11:15||Riki Eggert (King’s College, London): A chemical approach to understanding cell division|
|11:45||Matt Iadanza (University of Leeds): All the same but completely different: A new cryoEM fibril structure illustrating the diverse structural underpinnings of a common amyloid architecture|
|12:00||Claire Friel (University of Nottingham): How sequence specifies function across the kinesin superfamily: one engine, many machines.|
|12:15||Matthias Rief (Technical University of Munich): Single molecule mechanics of proteins|
|12:45 - 14:30||Lunch and posters (with exhibitors & CCPs): The Refectory|
|Session 6: The Great Hall (chair Helen Walden, University of Glasgow):|
|14:30||Hagan Bayley (University of Oxford): Translocation of biopolymers through pores|
|15:00||Yuji Goto (IPR, Osaka): Revisiting supersaturation as a factor determining amyloid fibrillation|
|15:15||John Briggs (LMB, Cambridge): Understanding the structures of viruses and vesicles using cryo-electron tomography.|
|15:45||Closing remarks & prizes|
|15:55 – 16:25||Refreshments (stalls will be open): Parkinson Court|
Brian Kobilka; Plenary Lecture: The Great Hall
|17:30||Public engagement and wine reception: Parkinson Court|
Please see below the talk titles and speaker biographies.
“Just a brief message to thank you and say how much I enjoyed the Astbury Conversation. It was one of the best meetings I've been to in recent years - a great set of speakers (some in areas I know well and others who widened my horizons), a very positive environment and a length of meeting that fits in well with busy teaching schedules. It was also nice to see people that I hadn't seen for years.”
Delegate from 2016 Astbury conversation
Brian Kobilka, MD is Professor of Molecular and Cellular Physiology, and Hélène Irwin Fagan Chair in Cardiology at Stanford University School of Medicine. He received a Bachelor of Science Degree in Biology and Chemistry from the University of Minnesota, Duluth in 1977. He graduated from Yale University School of Medicine in 1981, and completed residency training in Internal Medicine at the Barnes Hospital, Washington University School of Medicine, St. Louis, Missouri in 1984. From 1984-1989 he was a postdoctoral fellow in the laboratory of Robert Lefkowitz at Duke University. In 1990 he joined the faculty of Medicine and Molecular and Cellular Physiology at Stanford University.
Research in the Kobilka lab focuses on the structure and mechanism of action of G protein coupled receptors (GPCRs), which constitute the largest family of receptors for hormones and neurotransmitters in the human genome. GPCRs are the largest group of targets for new therapeutics for a very broad spectrum of diseases. In 2012, Kobilka was awarded the Nobel Prize in Chemistry for his work on GPCRs. He is a member of the National Academy of Sciences, the National Academy of Medicine, and the American Academy of Arts and Sciences.
Katrin Rittinger is a senior group leader at the Francis Crick Institute in London. She obtained a degree in chemistry from the University of Heidelberg, Germany and went on to do a PhD at the Max Planck Institute for Medical Research in Heidelberg.
After a short postdoc at the Max Planck Institute for Molecular Physiology in Dortmund, Germany, she obtained an EMBO Long-term and a Marie Curie Fellowship to join the MRC-NIMR in London for a second postdoc, working on the structural characterisation of 14-3-3/ligand complexes and the regulation of Rho family GTPases.
In 2000 she established her own research group and has since studied a number of protein assemblies that regulate multiple aspects of signal transduction using biochemical and structural approaches. Her current work is focussed on the role of ubiquitination in the regulation of immune and inflammatory signalling pathways, with an emphasis on the function and mechanism of E3 ubiquitin ligases.
Carol holds the Chair of Dr. Lee’s Professor of Chemistry at the University of Oxford. She is recognised for using mass spectrometry to further research into the 3D structure of proteins and their complexes.
During her early research Carol developed and applied mass spectrometry to show how protein folding could be monitored in the presence of molecular chaperones. This research prompted her to find new ways to preserve mega Dalton complexes in the gas phase and led her to uncover the heterogeneity and dynamics of numerous multi protein complexes. In recent work she demonstrated the numerous roles played by lipids in regulating the structure and function of membrane protein assemblies. Her current interest is in uncovering the synergy of lipid and drug binding. With this information she is exploring new ways to characterise receptor-signalling complexes.
Carol’s graduate education was completed whilst working full-time in industry. She was subsequently admitted to the University of Cambridge where she completed her PhD in two years. Following an eight-year career break to begin raising her three children, she returned to research at Oxford. In 2001 she became the first female Professor in Chemistry at the University of Cambridge, returning to Oxford in 2009 to take up the Chair of Dr. Lee’s Professor of Chemistry.
Her research has attracted international awards and prizes including the Anfinsen Award from the Protein Society, the Biemann Medal from the American Society of Mass Spectrometry, the Davy Medal and the Rosalind Franklin Award from the Royal Society, the HUPO Award for Distinguished Achievement, the Anatrace Award from the American Biophysical Society, the Kaj Lindström-Lang Prize from the Carlsberg Research Center and the Torbern Bergmann Award from the Swedish Chemical Society. Carol also holds four honorary doctorates and received a DBE in 2013 for her contributions to science and industry.
Ulrike Eggert is a chemical biologist who has been a Professor of Chemical Biology at King’s since 2015. She received her first degree in chemistry from the University of Oxford and her PhD in chemistry from Princeton University, working on vancomycin resistance with Professor Daniel Kahne. She then moved to Harvard Medical School as a Helen Hay Whitney Foundation postdoctoral fellow in the laboratory of Professor Tim Mitchison, where she first started research on cell division.
In 2006, she started her independent career as Assistant Professor at the Dana-Farber Cancer Institute and Harvard Medical School and moved to King’s College London in 2011. Riki’s group uses chemical biology and cell biology approaches to study cell division at the process, pathway, protein and metabolite levels. A recent focus has been on understanding the roles lipids, and especially their side chains, play in processes driven by the cytoskeleton.
Riki serves on several editorial and advisory boards and is an associate editor for Biochemistry. Her lab is currently funded by a Wellcome Investigator Award and an ERC Consolidator Grant.
Professor David Agard. A US biophysicist, David joined the faculty of the department of Biochemistry and Biophysics at the University of California, San Francisco in 1983. He is currently a Professor of Biochemistry & Biophysics, Professor of Pharmaceutical Chemistry, and an Investigator with the Howard Hughes Medical Institute.
David was the founding Director of the California Institute for Bioengineering, Biotechnology and Quantitative Biomedical Research in 2001, and was its UCSF Scientific Director from 2002-2006. He received his PhD in Biological Chemistry from the California Institute of Technology working with Robert Stroud, did a brief postdoc with John Sedat at UCSF and his main postdoctoral work at the MRC Laboratory of Molecular Biology in Cambridge with Richard Henderson.
Having a strong background in structural biophysics, David’s current work focuses on elucidating the mechanisms of assisted folding by the Hsp90 molecular chaperone system and the mechanism of microtubule nucleation. David has been instrumental in the development of direct phasing methods for SAXS, three dimensional deconvolution and Structured Illumination light microscopies, cryo-electron tomography, the K2 Summit single electron counting direct detector, and second-generation beam-induced motion correction software.
His work has been recognized by his election to the National Academy of Sciences in 2007 and American Academy of Arts and Sciences in 2009. Beyond numerous advisory boards, David served on the National Advisory General Medical Sciences Council at the NIH.
Richard Bayliss joined the University of Leeds in 2016 as a Professor in the Faculty of Biological Sciences. He graduated from the University of Cambridge with a first degree in Natural Sciences, and a PhD based on his research at the MRC Laboratory of Molecular Biology. After periods as a Research Fellow at Trinity College and an EMBO Fellow at EMBL in Heidelberg, Germany, he returned to the UK as a postdoctoral researcher at Birkbeck College, London.
In 2005, he was awarded a Royal Society University Research Fellowship to establish his own research group at the Institute of Cancer Research in London. He moved to the University of Leicester in 2011, and was awarded a Personal Chair in 2014.
Richard works at the interface of structural, cell, chemical and cancer biology, studying cell division and signaling pathways involving protein kinases and intrinsically disordered proteins. He collaborates extensively with cancer biologists, clinicians and cancer drug discovery groups across the UK and internationally.
Hagan Bayley is the Professor of Chemical Biology at the University of Oxford. Major interests of his laboratory are the development of engineered pores for stochastic sensing, the study of covalent chemistry at the single molecule level, ultrarapid DNA sequencing and the fabrication of synthetic tissues.
In 2005, Dr. Bayley founded Oxford Nanopore to exploit the potential of stochastic sensing technology. The company has developed the MinION portable DNA sequencer. In 2014, he founded OxSyBio to build synthetic tissues for regenerative medicine.
John Briggs is a Group Leader at the MRC Laboratory of Molecular Biology in Cambridge. Briggs completed his DPhil in Structural Biology at Oxford University, UK in the Lab of Stephen Fuller, where he performed cryo-electron microscopy of retroviruses. After a short postdoc in Munich, in 2006 he set up his own research group at the European Molecular Biology Laboratory, Heidelberg.
His group has worked on understanding the structure and the assembly/disassembly mechanisms of COPI, COPII and clathrin coated vesicles and of viruses including HIV-1 and influenza. Briggs’ group has developed and optimized methods for cryo-electron tomography and for correlative light and electron microscopy. This work has been recognized by honours including the Royal Microscopical Society Medal for Life Sciences, the Ernst-Ruska Prize for Electron Microscopy, and election to EMBO membership. His lab moved to the LMB in January 2017.
Charalampos Babis Kalodimos is the Chair of the Structural Biology Department at St Jude Children’s Research Hospital and holds the Joseph Simone Endowed Chair in Basic Research. He obtained his bachelor degree from University of Ioannina in Greece and his PhD from the Institut Curie in Paris. From 1999-2003 he worked as a postdoctoral fellow in the group of Robert Kaptein in Utrecht, The Netherlands, where he was introduced in the world of biomolecular NMR.
His group works on two main directions: first, the determination of the structural and dynamic basis for the function and assembly of large protein machineries; and second, the determination of the role of internal protein dynamics in regulating protein activity and allosteric interactions.
He has received numerous awards including the Young Investigator Awards from the Protein Society, the Biophysical Society, and the New York Academy of Sciences, the Stig Sunner Award and the Raymond and Beverly Sackler International Prize in the Physical Sciences.
Talk title: Enzymatic manipulation of peptides: making what is hard look easy
Jim Naismith, FRS FRSE FMedSci is a structural and chemical biologist. He left school aged 16 in 1985, graduated from Edinburgh University in 1989 with a BSc in Chemistry and a PhD in 1992 from University of Manchester. He spent two years in the lab of Steve Sprang, Dallas Texas, as a NATO Fellow.
In January 1995 he came back to the UK and took a lectureship at St Andrews, where he has been since. He was Director of the Biomedical Science Research Complex at St Andrews, doubling its size (2009-2016). His research focus is enzyme function and carbohydrate synthesis and translocation in bacteria. At the core of his work is the use of structures to illuminate molecular transformations.
He has served the wider community through Chairmanship of CCP4, SFX (the UK contribution to building a beamline at the European X-ray Free election laser) and for nearly 20 years in different roles as advisor to Diamond.
Talk title: Nature-inspired approaches for bioactive small molecule discovery
Adam Nelson has been Professor of Chemical Biology at the University of Leeds since 2005. He obtained his first degree (Natural Sciences; 1993) and PhD (in synthetic organic chemistry; 1996) from the University of Cambridge. He joined the University of Leeds as a lecturer in organic chemistry in 1998, and was Director of the Astbury Centre for Structural Molecular Biology at Leeds between 2009 2011.
His highly collaborative research programme focuses on the application of synthetic chemistry to problems ranging from the discovery of chemical probes of biological mechanisms to the directed evolution of synthetically-valuable enzymes. He currently holds an EPSRC Established Career Fellowship (2016-2021) focusing on the realisation of an autonomous approach to functional small molecule discovery. Adam currently supervises 11 PhD students and 9 postdoctoral fellows, and holds a range of local, national and international leadership roles.
Talk title: Single molecule mechanics of proteins
Matthias Rief obtained his PhD in Physics in 1997 at the Ludwig-Maximilians-Universität München, Germany, He continued his studies with a DFG-sponsored postdoctoral fellowship at Stanford University in the laboratory of J. A. Spudich focussing on the structure and function of molecular motors.
Since 2003, Matthias Rief has been a full professor of Biophysics at the Technische Universität München. Matthias Rief is an expert in single molecule force spectroscopy of biomolecules. He has made contributions to the understanding of the mechanics of molecular motors and folding and unfolding mechanics of proteins. Prof. Rief has been recognized with a number of awards, including the Jahrespreis of the German Biophysical Societ and the Heinz Maier-Leibnitz Prize from the DFG.
He is a member of the German National Academy of Sciences Leopoldina and of the Bavarian Academy of Sciences.