Career History

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. 

 

My topic of research is protein structure, protein dynamics and protein function and we employ a variety of computational techniques, including simulation methods and bioinformatics.  A particular focus of my research is on protein domain movements and our DynDom webserver (www.cmp.uea.ac.uk/dyndom) is the world’s foremost site for the analysis of protein domain movements.

 

I collaborate with colleagues in Japan and was awarded a JSPS Bridge Fellowship in 2015, a JSPS London Furusato Award in 2009, a JSPS Invitation Fellowship for Research in Japan (Short Term) in 2007, and a Royal Society Outgoing Short Visit grant to visit colleagues in Japan, particularly my long-term collaborator Professor Akio Kitao at the Institute of Molecular and Cellular Biosciences, University of Tokyo.

 

At the School of Computing Sciences, I work with Dr Stephen Laycock on the development of haptic (force-feedback)-based tools for the study of biomolecular interactions (www.haptimol.com) and with Dr Gavin Cawley using machine learning techniques for the study of protein domain movements.

Academic Background

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 on Protein Secondary Structure Prediction at the Department of Molecular Biology at the University of Edinburgh, Scotland, before embarking on my research career.

Highlighted Publications

See All

Hayward, S., Kitao, A.

(2015)

Monte Carlo sampling with linear inverse kinematics for simulation of protein flexible regions,

in Journal of Chemical Theory and Computation

11.

pp. 3895–3905

Full Text UEA Repository

(Article)

(Published)


Iakovou, G., Hayward, S., Laycock, S.

(2014)

A real-time proximity querying algorithm for haptic-based molecular docking,

in Faraday Discussions

169.

pp. 359-377

Full Text UEA Repository

(Article)

(Published)


Taylor, D., Cawley, G., Hayward, S.

(2014)

Quantitative method for the assignment of hinge and shear mechanism in protein domain movements,

in Bioinformatics

30.

pp. 3189-3196

Full Text UEA Repository

(Article)

(Published)


Yura, K., Hayward, S.

(2009)

The interwinding nature of protein-protein interfaces and its implication for protein complex formation,

in Bioinformatics

25.

pp. 3108-3113

Full Text UEA Repository

(Article)

(Published)


Hayward, S.

(1999)

Structural Principles Governing Domain Motions in Proteins,

in Proteins, Structure, Function and Genetics

36.

pp. 425-435

UEA Repository

(Article)

(Published)


Hayward, S., Berendsen, H. J. C.

(1998)

Systematic Analysis of Domain Motions in Proteins from Conformational Change: New Results on Citrate Synthase and T4 Lysozyme,

in Proteins, Structure, Function and Genetics

30.

pp. 144-154

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Kitao, A., Go, N.

(1995)

Harmonicity and Anharmonicity in Protein Dynamics: A Normal Mode Analysis and Principal Component Analysis,

in Proteins, Structure, Function and Genetics

23.

pp. 177-186

UEA Repository

(Article)

(Published)


All Publications

See Highlights
<- Page 1 of 3 ->

Matthews, N., Easdon, R., Kitao, A., Hayward, S., Laycock, S.

(2017)

High quality rendering of protein dynamics in space filling mode,

in Journal of Molecular Graphics and Modelling

78

pp. 158-167

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Milner-White, E. J.

(2017)

Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments,

in Proteins: Structure, Function, and Bioinformatics

85

(10)

pp. 1866–1881

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Milner-White, E.

(2017)

Cover Image, Volume 85, Issue 10 (page C1),

Full Text

(Other contribution)

(Published)


Iakovou, G., Hayward, S., Laycock, S.

(2017)

Virtual environment for studying the docking interactions of rigid biomolecules with haptics,

in Journal of Chemical Information and Modeling

57

(5)

pp. 1142–1152

Full Text UEA Repository

(Article)

(Published)


Iakovou, G., Laycock, S., Hayward, S.

(2016)

Determination of locked interfaces in biomolecular complexes using Haptimol_RD,

in Biophysics and Physicobiology

13

pp. 97-103

Full Text UEA Repository

(Article)

(Published)


Girdlestone, C., Hayward, S.

(2015)

The DynDom3D webserver for the analysis of domain movements in multimeric proteins,

in Journal of Computational Biology

23

(1)

pp. 21-26

Full Text UEA Repository

(Article)

(Published)


Iakovou, G., Hayward, S., Laycock, S. D.

(2015)

Adaptive GPU-accelerated force calculation for interactive rigid molecular docking using haptics,

in Journal of Molecular Graphics and Modelling

61

pp. 1-12

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Kitao, A.

(2015)

Monte Carlo sampling with linear inverse kinematics for simulation of protein flexible regions,

in Journal of Chemical Theory and Computation

11

(8)

pp. 3895–3905

Full Text UEA Repository

(Article)

(Published)


Iakovou, G., Hayward, S., Laycock, S.

(2014)

A real-time proximity querying algorithm for haptic-based molecular docking,

in Faraday Discussions

169

pp. 359-377

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Leader, D. P., Al-Shubailly, F., Milner-White, E. J.

(2014)

Rings and ribbons in protein structures: Characterization using helical parameters and Ramachandran plots for repeating dipeptides: Rings and Ribbons in Protein Structures,

in Proteins: Structure Function and Bioinformatics

82

(2)

pp. 230-239

Full Text UEA Repository

(Article)

(Published)


Taylor, D., Cawley, G., Hayward, S.

(2014)

Quantitative method for the assignment of hinge and shear mechanism in protein domain movements,

in Bioinformatics

30

(22)

pp. 3189-3196

Full Text UEA Repository

(Article)

(Published)


Taylor, D., Cawley, G., Hayward, S.

(2013)

Classification of Protein Domain Movements using Dynamic Contact Graphs,

in PLoS ONE

8

(11)

article no. e81224

Full Text UEA Repository

(Article)

(Published)


Stocks, M., Laycock, S., Hayward, S.

(2011)

Applying forces to elastic network models of large biomolecules using a haptic feedback device,

in Journal of Computer-Aided Molecular Design

25

(3)

pp. 203-211

Full Text UEA Repository

(Article)

(Published)


Hayward, S., James Milner-White, E.

(2011)

Simulation of the β- to α-sheet transition results in a twisted sheet for antiparallel and an α-nanotube for parallel strands: Implications for amyloid formation,

in Proteins: Structure, Function, and Bioinformatics

pp. n/a-n/a

Full Text UEA Repository

(Article)

(Published)


Hayward, S., Kitao, A.

(2010)

Effect of end constraints on protein loop kinematics,

in Biophysical Journal

98

(9)

pp. 1976-1985

Full Text UEA Repository

(Article)

(Published)


Laycock, S., Stocks, M., Hayward, S.

(2010)

Navigation and exploration of large data-sets using a haptic feedback device,

UEA Repository

(Paper)

(Published)


Stocks, M. B., Hayward, S., Laycock, S. D.

(2009)

Interacting with the biomolecular solvent accessible surface via a haptic feedback device,

in BMC Structural Biology

9

article no. 69

Full Text UEA Repository

(Article)

(Published)


Poornam, G. P., Matsumoto, A., Ishida, H., Hayward, S.

(2009)

A method for the analysis of domain movements in large biomolecular complexes,

in Proteins: Structure, Function, and Bioinformatics

76

(1)

pp. 201-212

Full Text UEA Repository

(Article)

(Published)


Qi, G., Hayward, S.

(2009)

Database of ligand-induced domain movements in enzymes,

in BMC Structural Biology

9

article no. 13

Full Text UEA Repository

(Article)

(Published)


Nishima, W., Qi, G., Hayward, S., Kitao, A.

(2009)

DTA: Dihedral transition analysis for characterization of the effects of large main-chain dihedral changes in proteins,

in Bioinformatics

25

(5)

pp. 628-635

Full Text UEA Repository

(Article)

(Published)


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Key Research Interests

The general area of my research concerns conformational change in proteins and protein structure.  In particular I am interested in the relationship between the two. We use various computational methods including, biogeometry, molecular dynamics simulation, and bioinformatics based approaches.

A main focus concerns domain motions in enzymes. Using molecular dynamics simulation we have shown that for some enzymes a domain-locking mechanism operates which keeps domains open in the absence of a functional ligand. The exact nature and purpose of the locking mechanism in alcohol dehydrogenase was elucidated recently.  

Another thread of my research on domain proteins concerns the creation of a database of protein domain movements based on my DynDom software (see http://www.cmp.uea.ac.uk/dyndom).  This is the foremost database for protein domain motions and forms the foundation to a bioinformatics based approaches to understanding protein conformational change.

We have recently become interested in the little known secondary structure alpha-sheet which was a structure predicted by Pauling and Corey in 1951 but hardly found in proteins at all.  However, recently interest in this “poor cousin” has been rekindled by the finding that it may be involved in amyloid diseases such as Alzheimer’s disease, Parkinson’s Huntington’s, Type II diabetes and the prion diseases such as BSE (mad cow).  We were the first to calculate the geometrical properties of a strand of alpha-sheet.

Steven Hayward is part of the Computational Biology Group

Selected Publications

Hayward, S. and Milner-White, E.J., The geometry of alpha-sheet: Implications for its possible function as amyloid precursor in proteins. Proteins-Structure, Function and Bioinformatics, Volume 71, Number 1, Page(s) 415 - 425, 2008.

Hayward, S. and Kitao, A., Molecular dynamics simulations of NAD+-induced domain closure in horse liver alcohol dehydrogenase. Biophysical Journal, Volume 91, Issue 5, Page(s) 1823-1831, 2006.

Qi, G., Lee, R., and Hayward, S., A comprehensive and non-redundant database of protein domain movements. Bioinformatics, Volume 21, Number 12, Page(s) 2832-2838, 2005.

Hayward, S., Identification of specific interactions that drive ligand-induced closure in five enzymes with classic domain movements. Journal of Molecular Biology, Volume 339, Issue 4, Page(s) 1001-1021, 2004.

Collaborators

Dr A. Kitao, University of Tokyo
Dr H. Ishida, Japan Atomic Energy Agency
Professor K. Yura, Ochanomizu University
Professor J. Milner-White, Glasgow
Dr Danilo Roccatano, Jakobs University, Germany
Dr Bert de Groot, Max Planck Institute for Biophysical Chemistry
Professor A. Day, UEA
Dr S. Laycock, UEA
Dr. A. Matumoto, Japan Atomic Energy Agency

Research Group Membership

Current members

Mr Daniel Taylor

Past members

Dr Guoying Qi
Dr Guru Poornam
Dr Catherine Snow

External Activities and Indicators of Esteem

  • Awarded Japan Society for the Promotion of Science Bridge Fellowship FY2014 to support 6 week research and networking visit to Japan, Feb 2015.
  • Regular invited speaker: Workshop on Molecular Theories and Simulations, Gaeta, Italy, May 2002-6
  • Invited speaker: Theory and simulation of biomolecular nano-machines International Conference, Kobe, Japan 2006
  • Visiting scientist: Information Technology Based Laboratory (ITBL), Japanese Atomic Energy Agency (JAEA), Kizu, Japan, 2003 and 2007

Key Responsibilities

Library Liaison