Professor Mike Williamson

Department of Molecular Biology and Biotechnology

Head of Department

m.williamson@sheffield.ac.uk
+44 114 222 4224

Full contact details

Professor Mike Williamson
Department of Molecular Biology and Biotechnology
Profile

My research concentrates on protein structure and function, mainly by means of NMR, and is described in more detail below.

I also teach NMR and protein structure, signalling, membranes and molecular motors, as well as numerical and statistical methods. I was a reviewer for the HEFCE QAA Molecular Biosciences reviews in 1998-2000, and coincidentally led the MBB submission, in which we got 24/24.

I also headed up the departmental Independent Evaluation of Teaching in 2008, which was also highly complimentary of our teaching. I have been involved in a number of University committees, mostly on admissions, finance and personnel.

I was (2009-2011) Chair of the UK NMR discussion group; also (2009-2012) Chair of the Biochemical Society theme panel II (Molecular structure and function);  (2009-2013) a member of BBSRC Committee D (Molecules, Cells and Industrial Biotechnology); and (2005-2009) secretary of Euromar.

I was on sabbatical in Osaka, Japan from September 2008 until September 2009, mainly to write a book, entitled How Proteins Work, published by Garland Press in July 2011 and available online and in all good bookshops. Also available in Italian and Japanese translations.

Career history

  • 1975-1978 Natural Sciences, Clare College, Cambridge University (I)
  • 1978-1981 PhD "Structural Studies on Some Antibiotics", supervised by Dudley Williams
  • 1981-1984 Junior Research Fellow, Churchill College, Cambridge
  • 1992-1983 SERC/NATO overseas research fellow, ETH Zürich, with Kurt Wüthrich
  • 1984-1990 Team leader, Bio-NMR, Roche Products Ltd, Welwyn Garden City
  • 1990-current University of Sheffield (appointed Professor in 2001)
  • 2017  Head of Department of Molecular Biology and Biotechnology
  • 1995 Fellow of the Royal Society of Chemistry and chartered chemist
  • 1997 Japan Society for the Promotion of Science (JSPS) invitation fellow
  • 2001 ScD, University of Cambridge
  • 2008-9 Visiting professor, Kinki University, Japan
  • 2009 Visiting professor, Osaka University, Japan
  • 2015 Special invited professor, Kyoto University, Japan
Research interests

During my PhD I used NMR to look at the structure and interactions of antibiotics mainly related to vancomycin, still a vital drug in the constant battle against bacterial drug resistance. This led to an interest in the NOE, where I worked first on 1D NOEs, showing that by using a viscous solvent you can make small molecules behave like bigger ones, and determined the definitive structure of vancomycin.

Around this time, Wüthrich was developing 2D NMR as a way of studying proteins, so after my PhD I got a research fellowship to work in his lab, where I was lucky enough to work on the first NMR structure of a globular protein (see his 2002 Nobel Prize lecture).

Since then, I have worked both on NMR methodology and on determination of protein structures by NMR. In methodology, I have worked in four main areas:

  • The nuclear Overhauser effect (NOE)
  • Chemical shifts in proteins
  • Relaxation
  • Study of proteins using high pressure
Publications

Show: Featured publications All publications

Journal articles

All publications

Books

Journal articles

Chapters

Conference proceedings papers

  • Nance CL, Williamson MP, McCormick TG, Paulson SM & Shearer WT (2006) Epigallocatechin gallate, green tea catechin, binds to the T cell receptor, CD4. JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, Vol. 117(2) (pp S325-S325) RIS download Bibtex download
  • Nance CL, Williamson MP, McCormick TG & Shearer WT (2005) Binding of the green tea polyphenol, epigallocatechin gallate, to the CD4 receptor on human CD4+ T cells resulting in inhibition of HIV-1-gp120 binding. CLINICAL IMMUNOLOGY, Vol. 115 (pp S245-S246) RIS download Bibtex download
  • Miyauchi S, Nakazawa Y, Suzuki Y, Kurashina M, Sato H, Asakura T & Williamson MP (2005) Change in orientation and dynamics of DMPC molecules induced by aggregation of Aβ (1-40) molecules studied using solid state and solution NMR. Polymer Preprints, Japan, Vol. 54(2) (pp 4983) RIS download Bibtex download
  • Nakazawa Y, Suzuki Y, Miyauchi S, Sato H, Williamson MP, Ando I & Asakura T (2005) Structural and dynamical studies of Aβ(1-40)-Ganglioside system with solid state and solution NMR. Polymer Preprints, Japan, Vol. 54(1) (pp 727) RIS download Bibtex download
  • Williamson MP (2003) Solving the first globular protein structure: BUSIIIA. MAGNETIC RESONANCE IN CHEMISTRY, Vol. 41 (pp S64-S69) RIS download Bibtex download
  • Haslam E, Williamson M & Charlton A (2000) Protein-polyphenol interactions. International Congress and Symposium Series - Royal Society of Medicine(226) (pp 25-33) RIS download Bibtex download
  • Asakura T, Iwadate M, Demura M & Williamson MP (1999) Structural analysis of silk with C-13 NMR chemical shift contour plots. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, Vol. 24(2-3) (pp 167-171) RIS download Bibtex download
  • Williamson MP, Simpson PJ, Bolam DN, Hazlewood GP, Ciruela A, Cooper A & Gilbert HJ (1999) How the N-terminal xylan-binding domain from C-fimi xylanase D recognises xylan. RECENT ADVANCES IN CARBOHYDRATE BIOENGINEERING(246) (pp 212-220) RIS download Bibtex download
  • Charlton AJ, Baxter NJ, Haslam E & Williamson MP (1998) Salivary proteins as a defence against dietary tannins. COST 916 - POLYPHENOLS IN FOOD (pp 179-185) RIS download Bibtex download
  • Charlton AJ, Baxter NJ, Haslam E & Williamson MP (1998) Salivary proline-rich proteins as a defence against dietary tannins. COST 916 - POLYPHENOLS IN FOOD (pp 201-201) RIS download Bibtex download
  • PICKETT MW, WILLIAMSON MP & KELLY DJ (1994) AN ENZYME AND C-13-NMR STUDY OF CARBON METABOLISM IN HELIOBACTERIA. PHOTOSYNTHESIS RESEARCH, Vol. 41(1) (pp 75-88) RIS download Bibtex download
  • Madison VS, Fry DC, Wegrzynski BB, Williamson MP, Danho W, Heimer EP & Felix AM (1990) Derivation of solution conformers of peptide hormones via constrained molecular dynamics based on 2-D NMR data. Proceedings of the Annual Conference on Engineering in Medicine and Biology(pt 4) (pp 1612) RIS download Bibtex download
Research group

My laboratory uses NMR (and other methods where appropriate) to determine the structure and dynamics of proteins in solution and to study their interactions with ligands. In addition we are developing new methods for characterising structures. Further details are in my web page and in the publications list. Recent work includes:

We continue to study protein structures, particularly if this illustrates function. Recent targets include the PLAT domain of human polycystin-1, which we show to recognise phosphatidyl serine and PI4P in the membrane; the protein Mms6, which helps assemble magnetite particles in magnetotactic bacteria; and the Wbl protein (Figure), which uses an Fe-S cluster to sense NO in M. tuberculosis and hence evade host defences.

We have studied how proteins recognize polysaccharides such as starch, cellulose, xylan and peptidoglycan in bacterial cell walls: for example, the LysM module which recognises peptidoglycan and chitin, as found in bacterial and fungal cell walls and invertebrate exoskeletons.

We have been developing new tools; in particular the use of high hydrostatic pressure to stabilise partially unfolded structures, and thus investigate functional conformational change in proteins. We have started looking at Rheo-NMR, to see how proteins align and aggregate in laminar flow.

We collaborate with numerous groups. These include a logstanding collaboration with Tetsuo Asakura on silk structure; a collaboration with Jim Thomas on ruthenium-based complexes that bind B-DNA and quadruplexes; a collaboration with Robert Poole on the so-called Carbon Monoxide Releasing Molecules (CORMs); and a study on how Hofmeister ions stabilise and/or solubilise proteins.

We have a longstanding interest in polyphenols such as those from tea, and in how they interact with the body. As part of this study, we have shown that the main component of green tea, epigallocatechin gallate (EGCG), has the potential to slow down HIV infection; and that EGCG can be transported effectively by binding to albumin in the blood.

Teaching activities

Level 4

  • MBB405 Advanced Research Topics

Level 3

  • MBB301 Dynamic proteins - motor proteins and their tracks (Module Coordinator)
  • MBB334 Biochemical Basis of Human Disease - amyloid disease, obesity and inflammation
  • MBB343 Biochemical Signalling - principles, receptor tyrosine kinases, Notch and NF-kB

Level 2

  • MBB266 Biostructures, Energetics and Synthesis