Projects per year
- Work package leader on Elixir Implementation Study "Building on PDBe-KB to chart and characterize the conformational landscape of native proteins". Awarded June 2021.
- Speaker at the ELIXIR 3D BioInfo Annual Meeting. Title of talk "Characterizing protein regions with different flexibility properties and their link to sequence and functional annotations." November 2021.
- Daiwa Foundation Small Grant for exchange visit to Professor Akio Kitao at the Tokyo Institute of Technology. Project titie: "Support for reciprocal visits by academics at the University of East Anglia and Tokyo Institute of Technology developing a system to educate and engage students in the principles of biomolecular interactions using a new virtual reality tool that engages the senses of sight and touch", January to December 2020.
- Awarded Japan Society for the Promotion of Science Bridge Fellowship FY2014 to support 6 week research and networking visit to Japan, Feb 2015.
Key Research Interests and Expertise
The general area of my research concerns protein structure and protein conformational change. In particular I am interested in the relationship between the two and their relationship to function. We use various computational methods including, biogeometry, molecular dynamics simulation, and bioinformatics based approaches.
We have created of a database of protein domain movements based on my DynDom software (see http://www.cmp.uea.ac.uk/dyndom) which is the foremost repository for this important class of protein conformational change. I am now working with colleagues across Europe in an Elixir implementation study to enable visitors to the PDBeKB database on protein structures to be presented with information that aids understanding of protein conformational change and its relationship to structure and function.
I also work with Professor James Milner-White and Professor Akio Kitao on the structure of amyloid. Amyloid is a misfolded form of protein that causes diseases such as Alzheimer’s, Parkinson’s, Huntington’s, Type II diabetes and the prion diseases such as BSE (mad cow). With Professor Milner-White I have been studying the little-known secondary structure "α-sheet" which has been proposed to play a role in the formation of the highly toxic amyloid intermediate. We were the first to calculate the geometry of a strand of α-sheet which was predicted by Pauling and Corey in 1951. Professor Kitao and I have been performing simulations on the Alzheimer's amyloid-β protein and have made some important insights on the structural determinants of fibril structures and how familial mutations might impact the resulting morphology of fibrils and intermediates.
I work with Dr Stephen Laycock and Dr Georgios Iakovou on the development of interactive protein docking tools. Many of these tools use a haptic force-feedback device to aid rapid exploration. In developing these tools we have made a number of important breakthroughs in exploiting the modern GPU for rapid calculation of interaction forces and of the conformational response to these forces. We have recently developed our DockIT tool for use with a VR head-mounted display. The tools can be downloaded from www.haptimol.co.uk.
Steven Hayward is part of the Computational Biology Group
R Veevers, G Cawley, S Hayward, Investigation of sequence features of hinge-bending regions in proteins with domain movements using kernel logistic regression, BMC Bioinformatics 21 (1), 1-18, 2020.
D Taylor, G Cawley, S Hayward, Quantitative method for the assignment of hinge and shear mechanism in protein domain movements, Bioinformatics 30 (22), 3189-3196, 2014.
D Roccatano, S Hayward, Free Energy Profile of Domain Movement in Ligand-Free Citrate Synthase, Journal of Physical Chemistry B 123 (9), 1998-2004, 2019.
RA Lee, M Razaz, S Hayward, The DynDom database of protein domain motions, Bioinformatics 19 (10), 1290-1291, 2003.
S Hayward, A Kitao, The role of the half-turn in determining structures of Alzheimer’s Aβ wild-type and mutants, Journal of Structural Biology, 213(4), 107792, 2021.
S Hayward, EJ Milner‐White, The geometry of α‐sheet: Implications for its possible function as amyloid precursor in proteins, Proteins: Structure, Function, and Bioinformatics 71 (1), 415-425, 2008.
G Iakovou, M Alhazzazi, S Hayward, SD Laycock, DockIT: a tool for interactive molecular docking and molecular complex construction, Bioinformatics 36 (24), 5698-5700, 2020.
N Matthews, A Kitao, S Laycock, S Hayward, Haptic-assisted interactive molecular docking incorporating receptor flexibility, Journal of Chemical Information and Modeling 59 (6), 2900-2912, 2019.
Professor A. Kitao, Tokyo Institute of Technology
Professor K. Yura, Ochanomizu University
Professor J. Milner-White, Glasgow
Dr Danilo Roccatano,University of Lincoln
Dr S. Laycock, UEA
Dr G. Iakovou, Aviva (Visiting Researcher at UEA)
Dr G. Cawley, UEA
- Director of Innovation
- Deputy Director of Research
- Chair of Postgraduate Taught Examination Board
I joined UEA as a joint lecturer in the School of Computing Sciences and the School of Biological Sciences in 1999 after spending postdoctoral years in two of the world’s leading groups in computational biomolecular research. I spent four years in the group of Professor Nobuhiro Go at the Department of Chemistry, University of Kyoto, Japan, and a further four years in the group of Professor Herman Berendsen at the Department of Chemistry, University of Groningen, The Netherlands. These postdoctoral positions were funded by personal fellowships: a Japan Society for the Promotion of Science (JSPS) Postdoctoral Fellowship, a European Commission Science and Technology Programme Fellowship for Japan, and a European Commission's Biotechnology Programme Fellowship.
I have a BSc(Hons) in Physics from the University of Bristol and a Diplom in Physics (6-year undergraduate degree) from Johannes-Gutenberg University, Mainz, Germany. I did a PhD at the Department of Molecular Biology at the University of Edinburgh, Scotland, before embarking on my research career.
Building on PDBe-KB to chart and characterize the conformational landscape of native proteins (UK-2021-3DBioInfo)
1/06/21 → 31/05/23
24/01/15 → 9/03/15
24/01/15 → 9/03/15
14/11/09 → 20/11/09
Hayward, S. & Kitao, A., 2015, In: Journal of Chemical Theory and Computation. 11, 8, p. 3895–3905 11 p.
Research output: Contribution to journal › Article › peer-review8 Citations (Scopus)
Taylor, D., Cawley, G. & Hayward, S., 15 Nov 2014, In: Bioinformatics. 30, 22, p. 3189-3196 8 p.
Research output: Contribution to journal › Article › peer-reviewOpen AccessFile34 Citations (Scopus)3 Downloads (Pure)
Iakovou, G., Hayward, S. & Laycock, S., 3 May 2014, In: Faraday Discussions. 169, p. 359-377 9 p.
Research output: Contribution to journal › Article › peer-reviewOpen AccessFile9 Citations (Scopus)6 Downloads (Pure)
The interwinding nature of protein-protein interfaces and its implication for protein complex formationYura, K. & Hayward, S., 2009, In: Bioinformatics. 25, 23, p. 3108-3113 6 p.
Research output: Contribution to journal › Article › peer-reviewOpen Access15 Citations (Scopus)
Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozymeHayward, S. & Berendsen, H. J. C., 1 Feb 1998, In: Proteins, Structure, Function and Genetics. 30, 2, p. 144-154 11 p.
Research output: Contribution to journal › Article › peer-review689 Citations (Scopus)