Key Research Interests and Expertise

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  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.


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

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