williamsonm

Professor Mike Williamson

Head of Department


Tel: 0114 222 4224
Email: m.williamson@sheffield.ac.uk

Research

Research Precis

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, linked on the right. Recent work includes:

fig1

We have been developing new tools to characterise volume fluctuations in proteins, which occur on timescales between ns and ms. In particular, we have shown that changes in the NMR spectrum resulting from hydrostatic pressures of up to 2 kbar can be used to show how proteins move, and also how they start to denature under pressure. The mobilities are greatest at the active site, and usually involve buried water molecules, which are very important for increasing local flexibility (Figure 1).

We have demonstrated that exposed salt bridges are not energetically favourable in solution, even though they are often observed in crystals.

In collaboration with Prof Hunter in MBB, we have determined structures for two trans-membrane proteins involved in bacterial light-harvesting. The structures are very similar in organic solvents and in micelles. These structures have been used to model the intact photosynthetic complex.

We have studied how proteins recognize polysaccharides such as starch, cellulose and xylan. The activities of enzymes that degrade these plant polymers tend to be organized into ‘cellulosomes’ which are large assemblies of many different enzymes. We have determined the structure of the key assembly component of the anaerobic cellulosome and showed that it probably relies on protein / carbohydrate recognition to assemble. We have also looked at the LysM module which recognises peptidoglycan and chitin, as found in bacterial and fungal cell walls and intertebrate exoskeletons.

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, has the potential to slow down HIV infection.

Research Keywords

NMR spectroscopy, structural biology, biochemistry

You can apply for a PhD position in MBB here.

Contact me at M.Williamson@sheffield.ac.uk for further information.



Metabolomic studies of E. coli adaptation from anaerobic to aerobic growth Escherichia coli is a commensal organism that lives in the human gut. Occasionally it gives rise to food poisoning incidents, but mainly it is important for digestion and uptake of nutrients. In the gut it has an anaerobic lifestyle. On passage from the body, it is exposed to an aerobic environment and has to adapt very rapidly in order to survive and compete. This requires a major change in the main metabolic pathways such as glycolysis and the TCA cycle. We propose to investigate how its metabolism changes by growing E. coli in chemostats under defined conditions, sampling it using rapid quenching of metabolism, and then investigate the metabolites using two-dimensional NMR supported by other techniques (such as mass spectrometry) as required. The aim is to derive as complete a map as possible of the time-dependent changes in metabolites on going from anaerobic to aerobic, and to model these changes in order to gain an understanding of the underlying changes in metabolic pathways. In parallel, we shall carry out molecular biology in order to label specific proteins and to delete key enzymes, to check whether the model is correct. A key aim is to investigate whether glycolytic enzymes are relocated to the cell membrane during the change from anaerobic to aerobic growth. The project will therefore provide training in a wide range of microbiological and molecular biological techniques, as well as analytical techniques, especially NMR.
Self-association of the Alzheimer’s peptide Aβ on membrane surfaces

Alzheimer’s disease is a neurodegenerative disease that is particularly common amongst the elderly. It accounts for about 65% of all cases of dementia, and affects about 6% of people over 65, rising to 50% of people over 85. As the number of elderly people rises, the incidence of Alzheimer’s is expected to increase, quadrupling by 2050. Alzheimer’s leads to memory loss and behavioural change. The cost to society is enormous, with the major burden falling on family members. There is currently no cure. The cause of the disease is generally thought to be a small peptide called Aβ, which is cleaved from a much larger protein of unknown function. Aβ is 40-43 residues long. In solution, it forms fibrils, which aggregate into plaques. Such plaques form the primary diagnosis of Alzheimer’s in post-mortems, but it is generally agreed that the plaques themselves are not the toxic species, which is some earlier stage of Aβ aggregation, generally described as oligomers. However, there is no agreed mechanism for how Aβ oligomers cause the disease.

The project investigates the hypothesis that it is self-association of Aβ oligomers on membrane surfaces that leads to Alzheimer’s. We will use nuclear magnetic resonance (NMR) as the primary tool to investigate this hypothesis, supported by biochemical assays and electron microscopy. The research plan involves:

  • Expression of Aβ(1-40) in E. coli and purification, using an established methodology
  • Mutagenesis of Aβ (by polymerase chain reaction) to create single cysteines, which can be used to attach spin labels to Aβ
  • Measurement of paramagnetic relaxation enhancements (PREs) for wild-type Aβ in the presence of a small amount of spin-labelled Aβ, to establish the geometry of the protofibrils. This will be done using both solution-generated fibrils and membrane-generated fibrils, to investigate the hypothesis that the two fibrils have different morphology (parallel and antiparallel β-sheets, respectively). We will also compare Aβ alone, and Aβ in the presence of membranes, to see if the membranes induce specific types of association.
  • Measurement of PREs for wild-type Aβ in the presence of spin-labelled small unilamellar vesicles, to establish how it interacts with membrane surfaces. This will be done using 13C-labelled Aβ, to investigate the hypothesis that lysine and aromatic sidechains are important for the interaction
  • The effect of metal ions and pH on these associations will be investigated, because both of these could be important mediators of the association
Structural biology of the intrinsically disordered protein SH2B1

Background

Signalling between the outside of the cell and the inside uses a complicated network of interacting systems. One common signalling mechanism uses receptor tyrosine kinases: binding of a ligand to the receptor causes dimerization of the receptor, which leads to the intracellular kinase domain on one receptor phosphorylating the kinase domain on its neighbour and activating it. The intracellular phosphorylation is recognised by a specific binding domain, often an SH2 domain, which acts to relay the signalling downstream and ultimately to lead to metabolic changes in the cell. In many cases, there are extra proteins involved that modify the signal response. SH2B1 is one of these. It is a large protein (670 amino acids) that contains an SH2 domain and binds to phosphorylated receptors. It also contains a PH domain (binds to membranes) and a self-dimerisation domain. The rest of the protein appears to be intrinsically disordered. Intrinsically disordered proteins (IDPs) often have weak intramolecular binding between folded domains and disordered sections, which alter the availability of binding sites, bring different parts of the protein closer together, create new interaction sites, and regulate protein-protein association (Williamson & Potts Biochem Soc Trans, 2012, 40:945-949). It is therefore likely that the IDP regions of SH2B1 have functions in controlling the association of ligands to target receptors, dependent on intramolecular interactions between IDP regions and folded domains. For example, there has been a publication describing a likely interaction between the SH2 domain and a sequence within residues 1-247.
SH2B1 binds to the insulin receptor, and also to several other related receptors including the leptin receptor, which has a function in regulating eating and obesity. Deletion of the gene for SH2B1 leads to severe obesity in mice, insulin resistance, age-dependent hyperinsulinaemia, hyperphagia [overeating], diabetes and glucose intolerance (DC Ren et al., Cell Metabol., 2005, 2:95-104; M Li et al., Endocrinology, 2006, 147:2163-2170.) It is therefore important, but its exact function is not well understood. The aim of the project is to study intramolecular interactions within SH2B1 and gain insights into how it works.

Outline of work to be undertaken

We will use polymerase chain reaction (PCR) to put restriction sites into the SH2B1 gene, cut out different parts of the gene, and insert them into E. coli, where they will be expressed with histidine tags so that we can use nickel affinity chromatography to purify the protein products. The proteins will be analysed by chromatography and NMR to see if they are folded. Folded regions may need some trimming at the ends to get them properly folded and without excessively long unfolded tails. They will then be expressed as isotopically labelled proteins and their NMR spectra will be assigned. The assignments will be used to define the secondary structure. Any novel proteins will have their structures determined.
We will analyse binding of IDP regions to the folded regions using chemical shift perturbation with 15N-labelled folded domains, which will give us interaction regions and affinities. Different lengths of IDP and different linker lengths will be studied to give us a clearer picture of intramolecular binding. If there is time, we will study dimerization of the dimerization domain and the effect of phosphorylation on affinities.

Teaching

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 and inflammation
MBB343 Biochemical Signalling - principles, receptor tyrosine kinases, Notch and NF-kB
MBB362 Biochemistry Data Handling

Level 2

MBB266 Biostructures, Energetics and Synthesis

Career History

Career History

  • 2017: Head of Department, Molecular Biology and Biotechnology
  • 2001 - present: Professor, University of Sheffield
  • 1993 - 2001: Reader, University of Sheffield
  • 1990 - 1993: Senior Lecturer, University of Sheffield
  • 1984 - 1990: Team Leader, Bio-NMR, Roche Products Ltd, UK
  • 1981 - 1984: Junior Research Fellow, Churchill College Cambridge, and SERC/NATO Overseas Research Fellow at ETH Zurich

Honours and Distinctions

  • 1975: Entrance scholar, Clare College Cambridge
  • 1981: Junior Research Fellow, Churchill College Cambridge
  • 1982: SERC/NATO Overseas Postdoctoral Fellow
  • 1997: Japan Society for the Promotion of Science (JSPS) Invitation Fellow
  • 1998 - 2000: Specialist reviewer in Molecular Biosciences for the Quality Assurance Agency
  • 2001: Sc.D., University of Cambridge
  • 2001 - 2004: Member of CCPN Executive Committee
  • 2001 - 2007: Council, Assessment and Qualifications Alliance (AQA)
  • 2004 - 2009: Secretary of EUROMAR
  • 2009 - 2012: Chair of Biochemical Society Theme Panel II (Molecular Structure)
  • 2009 - 2011: Chair of NMR Discussion Group
  • 2009 - 2014: Member of BBSRC Research Committee D
  • 2011: Teaching Prize, Dept of Molecular Biology and Biotechnology
  • 2015 - 2017: White Rose Doctoral Training Programme management board
  • 2016- present: Associate Editor, Biochemical Society Transactions
Personal Website

mikeMike Williamson's personal page

This page contains a more detailed summary of my research and interests than my main home page.


Brief CV

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

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 (for which I now look after the website); 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.bookcover


Research outline

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:

I have worked on a number of protein systems:

Carbohydrate binding modules (CBMs)

These are protein modules that are used to attach degradative enzymes to their substrate, such as starch, cellulose, xylan and other cell-wall constituents, and also used by bacteria to modify their own or other bacterial cell walls. Our main interest has been in how they recognise specifically their targets, which are chemically very similar: it turns out to be mainly steric rather than using hydrogen bonding. The work has mainly been structural, though we have also worried about enthalpy and entropy, and even a bit of enzymology.

The bacterial light-harvesting complex

This is a large membrane complex, which traps sunlight and feeds it to the reaction centre. We have used organic solvents and micelles to study some of the component peptides. When combined with other work, in particular electron microscopy and atomic force microscopy, together with a large body of mutagenesis and functional studies, this has allowed us to construct an atomic model of the entire complex.

Salivary proline-rich proteins and plant polyphenols

Salivary proline-rich proteins (PRPs) are the major proteins in parotid saliva. A major function appears to be to bind to plant polyphenols (tannins), which we consume in tea, coffee, wine and many fruits and cereals and are responsible for the sensation of astringency. They are unstructured proteins, so their binding is quite different from the more specific interactions that we are more used to seeing for proteins. The study has involved NMR as well as a wide range of other biophysical techniques.
This work has also led to two major and well-cited reviews of proline-rich regions (1994 and 2000), and a study suggesting that EGCG, the main polyphenol in green tea, may be able to slow down HIV infection. We also showed that albumin can transport large numbers of EGCG around the body, explaining why its half-life in the body is so long [Biosci Rep 2017 37]

The RegAB two-component signalling system

This is a classic bacterial two-component signalling system, in which an external stimulus (in this case oxygen tension) leads to phosphorylation of a membrane-bound kinase, which then phosphorylates an intracellular response regulator. The phosphorylated regulator undergoes a conformational change, binds to DNA and alters transcription. We expressed it in functional form, showed how it works, and how the DNA is recognised.

Silk

The structure of silk is surprisingly poorly understood. In a longstanding collaboration with Prof Tetsuo Asakura at the Tokyo University of Agriculture and Technology, we have worked on protein chemical shifts and also on methods for characterising silk structure, by solution state and solid state NMR. In the silk worm gland, silk is present in a form called Silk I; the better known fibrous form is called Silk II.We recently showed that the crystalline form of silk consists of two different packing arrangements in close proximity. The silk work led to a 2012 publication in Angewandte Chemie in which we show that antiparallel polyalanine crystallises in two different forms depending on its length. This is interesting first because it suggests that spider dragline silk may derive some of its remarkable strength from its polycrystalline form, and second because the completely linear strands have a rather different position in the Ramachandran plot compared to most beta strands: they are distinctly to the left of standard beta-sheet conformation. This suggests that (a) it takes very little energy to distort a beta-strand conformation, and (b) the phi/psi combination (particularly phi) looks to be strongly related to the twistedness of the strand.

In 2014/15 we published three significant papers. Two of these (Okushita et al (2014) Macromolecules 47:4308-16 and Asakura et al (2015) Macromolecules 48:28-36) show definitively that although silk II is indeed an antiparallel beta sheet, it has two different packings, both different from the classic model proposed by Pauling in 1955. The third (Asakura et al (2015) Macromolecules 48:2345-2357) is a review of what is now understood about the structures of silk I and silk II, particularly as understood from NMR.


We have recently started to be interested in the Hofmeister series. This is a rank ordering of anions, which affect protein stability and solubility. Anions at one end (eg sulphate, phosphate) tend to be highly charged, stabilise proteins but make them less soluble, and are often described as kosmotropes. Ions at the other end (eg thiocyanate) have low charge density, have the opposite effect, and are often called chaotropes. There is disagreement over how they work. We [Bye et al ACS Omega 2016 1:669-679] measured protein chemical shifts in the presence of Hofmeister ions and showed that they all bind, in similar places, though weakly; but that the Hofmeister effects are likely to be due to effects of the ions on water. Work is ongoing.

More recently we have started work on the signalling scaffold protein SH2B1, whhich contains large regions of intrinsically unstructured protein.


We have undertaken a variety of NMR-related projects, mostly with local academics. These include

  • in collaboration with Dr Jim Thomas in the Department of Chemistry at Sheffield, I have been studying the interaction of pyridophenazines with DNA, as a B-DNA duplex and also DNA quadruplexes. We have shown that that a quaternized derivative intercalates in an unusual sideways-on orientation, and also that the intercalation of a ruthenium derivative can be switched on and off by a single amino derivative; and that a bis-ruthenium derivative has significantly more affinity for quadruplexes than for B-DNA and so may turn out to be a useful probe for quadruplexes in the cell, particularly if chirally resolved
  • in an important collaboration with Prof Albert Ong in the Sheffield Medical School, we have been looking at polycystins 1 and 2 (responsible for the severe kidney disease Autosomal Dominant Polycystic Kidney Disease). By studying mutants and their interactions, we were able to show that they form coiled-coil dimerisation domains that interact [EMBO J 2010 29, 1176-1191]. We have gone on to look at the PLAT domain of PC-1. We have assigned the NMR spectrum, shown that it binds calcium, phosphatidyl serine and phosphatidyl inositol 4-phosphate, and that it regulates trafficking of PC-1 [J Am Soc Nephrol 2015, 27, 1159].
  • some definitive work on the cell wall of vegetative and germinating Bacillus subtilis [J. Bact. 1998 180, 4603-4612; J. Bact. 1999 181, 3956-3966; Biochemistry, 2003, 42, 257-264]
  • a collaboration with Prof Jeff Green on the protein Wbl [Nature Comms 2017 8:2280], which is a Fe-S protein produced by Mycoplasma tuberculosis that responds to the generation of NO by the host and turns on bacterial defence mechanisms.
  • studies on bacterial metabolism [Photosynthesis Research 1994 41, 75-88; Microbiology 2001, 147, 1473-1482; J Exp. Med. 2005 201 1637-1645; Mol. Micro. 2006 60 1262-1275]
  • a collaboration with Prof Robert Poole on CORMs (carbon monoxide-releasing molecules). These are ruthenium-based compounds that are widely believed to kill bacteria by releasing CO. Our work [Redox Biology, 2018, 18, 114-123] shows that they release very little CO, but that the Ru ions bind tightly to thiols (eg cysteine, glutathione) in the cell.
  • a collaborative study of bacterial metabolism using NMR-based metabolomics [PLoS One 2011 6(9):e25501], going on to show that under sudden aerobiosis, a glycolytic metabolome assembles on the cell membrane [Roy Soc Open Science 2016 3 160187]
  • synthesis and conformational studies of a nicked duplex decamer DNA, with Prof Lech Kozerski in Warsaw, Poland. This decamer has PEG6 tethers at each end, which means it can be made as a single molecule and has remarkable stability: Nucleic Acids Res. 2001 29, 1132-1143. It is also useful as a model for nicked DNA bound to topoisomerase I, for example to study binding of anticancer drugs such as topotecan Chem Eur J 2008 14, 2788-2794
  • a structure/function study on a bacterial Fasciclin I Domain Protein. This domain is found in a number of proteins that give rise to human disease (eg TGFBIp and periostin), and this study suggests a novel mechanism for how these domains function
  • as an offshoot on our work on chemical shifts, we have looked at salt bridges in protein G, in collaboration with Prof Poul Erik Hansen, and reached the important conclusion that exposed salt bridges are not populated in solution, by contrast to crystal structures, where they are of course common. We have also demonstrated the use of deuterium isotope shifts as a way of characterising the strength of hydrogen bonds, both experimentally and using ab initio calculations
  • studies on Aß, the peptide responsible for Alzheimer's disease. We showed that histidine 13 is crucial for correct interactions with ganglioside GM1 in lipid rafts [Biochem. J. 2006 397 483-490], and (in collaboration with Tetsuo Asakura) that Aß can insert into membranes [Chem. Phys. Lipids 2009 15854-60].

I have also written a number of reviews, including a recent Perspective on automated protein structure calculation, an update on NOEs in molecular biology, a survey of chemical shift perturbation (Progr NMR Spectrosc, 2013) [an ISI 'Highly Cited' paper], and a review on pressure-induced chemical shifts as probes for conformational fluctuations in proteins.


I am a keen musician (when I have the time!). I play jazz string bass and bass guitar, and have played the cello and bass, as a member of various orchestras, and also in quartets etc. for relaxation, though not recently.
I also rang bells, as a member of the band at Sheffield Cathedral, a 12-bell tower in the Yorkshire Association of Change Ringers.


List of publications

h-index of 54 (ISI WoS) and 11750 citations, or find me on google scholar, where I have an h-index of 65 and 17750 citations

As of March 2016, I had a pleasingly symmetrical publication profile on ISI Web of Science: 200 papers published or in press, just over 10000 citations (ie an average of 50 citations per paper), and an h-index of 50 (ie 50 papers with at least 50 citations).

First the NOE book referred to above:
The NOE in structural and conformational analysis, D Neuhaus and M P Williamson
Published by Wiley in 1989, and brought out in a completely revised and reprinted second edition in 2000.

And the recent book:
How Proteins Work, M P Williamson
Published by Garland Press in July 2011. This is a major new undergraduate text and available from all good bookstores (and online). It has been adopted as a course text by Universities including ANU and Sydney (Australia), Northwestern (USA), McMaster (Canada), Technical University of Denmark, and University of Tokyo. Reviews include 'a really nice book' (Chemistry World), 'really good', 'a great text', 'a great overview' (Amazon). Also published by Zanichelli in Italian, and Nankodo in Japanese.

A selection of early papers:

  • 'Structure of the antibiotic ristocetin A', D. H. Williams, V. Rajananda, G. F. Bojesen and M. P. Williamson, J. C. S. Chem. Commun. 1979, 906-8 my first paper!
  • 'Manipulation of the nuclear Overhauser effect by the use of a viscous solvent: the solution conformation of the antibiotic echinomycin', M. P. Williamson and D. H. Williams, J. C. S. Chem. Commun. 1981, 165-6 an influential paper, showing that the NOE can be made much larger by increasing the molecular correlation time
  • 'Structure revision of the antibiotic vancomycin. The use of nuclear Overhauser effect difference spectroscopy', M. P. Williamson and D. H. Williams, J. Amer. Chem. Soc. 1981, 103, 6580-5 for the first time, the correct structure of vancomycin, the last line of defence against MRSA
  • 'Interactions of vancomycin and ristocetin with peptides as a model for protein binding', M. P. Williamson, D. H. Williams and S. J. Hammond, Tetrahedron 1984, 40, 569-577 In which we developed several ideas later expanded and worked on extensively by the Williams group to understand intermolecular interactions
  • 'Solution conformation of the proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry', M. P. Williamson, T. F. Havel and K. Wüthrich, J. Mol. Biol. 1985, 182, 295-315 the first NMR structure of a globular protein, cited over 470 times
  • 'Secondary-structure dependent chemical shifts in proteins', M. P. Williamson, Biopolymers 1990, 29, 1423-31 in which I showed the structural significance of chemical shifts in proteins
  • 'Rapid pulsing artifacts in double-quantum filtered COSY', A. E. Derome and M. P. Williamson, J. Magn. Reson. 1990, 88, 177-185 a surprise hit, widely adopted as a standard method for DQF-COSY
  • 'Empirical comparisons of models for chemical shift calculation in proteins', M. P. Williamson and T. Asakura, J. Magn. Reson., Series B, 1993, 101, 63-71. one of several papers in which we developed methods for calculating chemical shifts in proteins
  • 'The structure and function of proline-rich regions in proteins', M. P. Williamson, Biochem. J., 1994, 297, 249-260 an important review
  • 'Application of 1H NMR chemical shifts to measure the quality of protein structures', M. P. Williamson, J. Kikuchi and T. Asakura, J. Mol. Biol., 1995, 247, 541-546 which demonstrates the importance of chemical shifts as a measure of structure quality
  • 'The relationship between amide proton chemical shifts and secondary structure in proteins', T. Asakura, K. Taoka, M. Demura and M. P. Williamson, J. Biomol. NMR, 1995, 6, 227-236 important because of the widespread use of HSQC spectra eg for chemical shift mapping
  • 'Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to ß-cyclodextrin', K. Sorimachi, M-F. Le Gal-Coeffet, G. Williamson, D. B. Archer and M. P. Williamson, Structure, 1997, 5, 647-661 an unusual structure because there are two functionally different binding sites
  • 'Temperature dependence of 1H chemical shifts in proteins', N. J. Baxter and M. P. Williamson, J. Biomol. NMR, 1997, 9, 359-369 still the best work out there (in my humble opinion) on temperature effects on HN protons
  • 'Characterisation of low free-energy excited states of proteins', N. J. Baxter, L. L. P. Hosszu, J. P. Waltho and M. P. Williamson, J. Mol. Biol. 1998, 284, 1625-1639 the work which set us on the path to studying protein excited states
  • 'The starch-binding domain from glucoamylase disrupts the structure of starch' S. M. Southall, P. J. Simpson, H. J. Gilbert, G. Williamson and M. P. Williamson, FEBS Letts, 1999, 447, 58-60 more or less my only enzymological paper, demonstrating the unusual role of the starch binding domain
  • 'Ca and Cß carbon-13 shifts in proteins from an empirical database', M. Iwadate, T. Asakura and M. P. Williamson, J. Biomol. NMR, 1999, 13, 199-211
  • 'The solution structure of Rb. sphaeroides LH1ß reveals two helical domains separated by a flexible region: Structural consequences for the LH1 complex' M. J. Conroy, W. Westerhuis, P. S. Parkes-Loach, P. A. Loach, C. N. Hunter and M. P. Williamson, J. Mol. Biol., 2000, 298, 83-94 atomic level details of a large membrane-bound complex
  • 'The structural basis for the ligand specificity of family 2 carbohydrate binding modules', P. J. Simpson, H. Xie, D. N. Bolam, H. J. Gilbert and M. P. Williamson, J. Biol. Chem., 2000, 275, 41137-41142 classic structure-activity combined with site-directed mutagenesis
  • 'The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains', B. K. Kay, M. P. Williamson and M. Sudol, FASEB J., 2000, 14, 231-241 another important review, cited over 750 times

Papers since 2001:

2001


Kozerski L, Mazurek AP, Kawecki R, Bocian W, Krajewski P, Bednarek E, Sitkowski J, Williamson MP, Moir AJ, Hansen PE
A nicked duplex decamer DNA with a PEG(6) tether
Nucleic Acids Res. 2001 29(5):1132-43

Iwadate M, Asakura T, Dubovskii PV, Yamada H, Akasaka K, Williamson MP
Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR
J Biomol NMR. 2001 19(2):115-24

Xie H, Bolam DN, Nagy T, Szabo L, Cooper A, Simpson PJ, Lakey JH, Williamson MP, Gilbert HJ
Role of hydrogen bonding in the interaction between a xylan binding module and xylan
Biochemistry. 2001 40(19):5700-7

Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ
Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A
Biochemistry. 2001 40(8):2468-77

Leighton MP, Kelly DJ, Williamson MP, Shaw JG
An NMR and enzyme study of the carbon metabolism of Neisseria meningitidis
Microbiology. 2001 147(6):1473-82

Xie H, Gilbert HJ, Charnock SJ, Davies GJ, Williamson MP, Simpson PJ, Raghothama S, Fontes CM, Dias FM, Ferreira LM, Bolam DN
Clostridium thermocellum Xyn10B carbohydrate-binding module 22-2: the role of conserved amino acids in ligand binding
Biochemistry. 2001 40(31):9167-76

Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP
Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi
Nat Struct Biol. 2001 8(9):775-8


2002

Jamieson SJ, Williamson MP, Abou-Hachem M, Nordberg KE, Simpson PJ
Virtually complete 1H, 13C and 15N resonance assignments of the second family 4 xylan binding module of Rhodothermus marinus xylanase 10A
J Biomol NMR. 2002 22(2):187-8

Charlton AJ, Baxter NJ, Khan ML, Moir AJ, Haslam E, Davies AP, Williamson MP
Polyphenol/peptide binding and precipitation
J Agric Food Chem. 2002 50(6):1593-601

Simpson PJ, Jamieson SJ, Abou-Hachem M, Karlsson EN, Gilbert HJ, Holst O, Williamson MP
The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase
Biochemistry. 2002 41(18):5712-9

Abou-Hachem M, Karlsson EN, Simpson PJ, Linse S, Sellers P, Williamson MP, Jamieson SJ, Gilbert HJ, Bolam DN, Holst O
Calcium binding and thermostability of carbohydrate binding module CBM4-2 of Xyn10A from Rhodothermus marinus
Biochemistry. 2002 41(18):5720-9

Potter CA, Ward A, Laguri C, Williamson MP, Henderson PJ, Phillips-Jones MK
Expression, Purification and Characterisation of Full-length Histidine Protein Kinase RegB from Rhodobacter sphaeroides
J Mol Biol 2002 320(2):201-13

Charlton AJ, Haslam E, Williamson MP
Multiple conformations of the proline-rich protein/epigallocatechin gallate complex determined by time-averaged nuclear Overhauser effects
J Am Chem Soc 2002 124(33):9899-905


2003

Jakeman DL, Ivory AJ, Blackburn GM, Williamson MP
Orientation of 1,3-bisphosphoglycerate analogs bound to phosphoglycerate kinase.
J Biol Chem 2003 278(13):10957-62

Horsburgh GJ, Atrih A, Williamson MP, Foster SJ.
LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major active glucosaminidase.
Biochemistry 2003 42(2):257-64

Refaee M, Tezuka T, Akasaka K, Williamson MP
Pressure-dependent changes in the solution structure of hen egg-white lysozyme
J Mol Biol 2003 327(4):857-65

Pell G, Williamson MP, Walters C, Du H, Gilbert HJ, Bolam DN
Importance of hydrophobic and polar residues in ligand binding in the family 15 carbohydrate-binding module from Cellvibrio japonicus Xyn10C
Biochemistry. 2003 42(31):9316-23

Williamson MP, Akasaka K, Refaee M
The solution structure of bovine pancreatic trypsin inhibitor at high pressure
Protein Sci. 2003 12(9):1971-9

Williamson MP
Many residues in cytochrome c populate alternative states under equilibrium conditions
Proteins. 2003 53(3):731-9

Laguri C, Phillips-Jones MK, Williamson MP
Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity
Nucleic Acids Res. 2003 31(23):6778-87


2004

Nakano E, Williamson MP, Williams NH, Powers HJ
Copper-mediated LDL oxidation by homocysteine and related compounds depends largely on copper ligation.
Biochim Biophys Acta. 2004 1688(1):33-42

Joebstl E, O'Connell J, Fairclough JP, Williamson MP
Molecular model for astringency produced by polyphenol/protein interactions.
Biomacromolecules. 2004 5(3):942-9

Bocian W, Kawecki R, Bednarek E, Sitkowski J, Pietrzyk A, Williamson MP, Hansen PE, Kozerski L
Multiple binding modes of the camptothecin family to DNA oligomers.
Chemistry, a European Journal. 2004 10(22):5776-87.


2005

Tunnicliffe RB, Bolam DN, Pell G, Gilbert HJ, Williamson MP
Structure of a mannan-specific family 35 carbohydrate-binding module: evidence for significant conformational changes upon ligand binding.
J Mol Biol. 2005 347(2):287-96

Exley RM, Shaw J, Mowe E, Sun Y-H, West NP, Williamson MP, Botto, M, Smith H, Tang CM
Available carbon source influences the resistance of Neisseria meningitidis against complement.
J Exp Med. 2005;201:1637-1645

Flint J, Bolam DN, Nurizzo D, Taylor EJ, Williamson MP, Walters C, Davies GJ, Gilbert HJ
Probing the mechanism of ligand recognition in family 29 carbohydrate binding
J Biol Chem. 2005 280:23718-23726

Williamson MP.
Systems biology: will it work?
Biochem Soc Trans. 2005 33(3):503-6

Joebstl E, Fairclough JP, Davies AP, Williamson MP
Creaming in black tea
J Agric Food Chem. 2005 53(20):7997-8002

Tunnicliffe RB, Waby JL, Williams RJ, Williamson MP
An experimental investigation of conformational fluctuations in proteins G and L
Structure. 2005 13(11):1677-84


2006

Leon-Kempis Mdel R, Guccione E, Mulholland F, Williamson MP, Kelly DJ
The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids
Mol Microbiol. 2006 60(5):1262-75

Potter CA, Jeong EL, Williamson MP, Henderson PJ, Phillips-Jones MK
Redox-responsive in vitro modulation of the signalling state of the isolated PrrB sensor kinase of Rhodobacter sphaeroides NCIB 8253
FEBS Lett. 2006 580(13):3206-10

Joebstl E, Howse JR, Fairclough JP, Williamson MP
Noncovalent Cross-Linking of Casein by Epigallocatechin Gallate Characterized by Single Molecule Force Microscopy
J Agric Food Chem. 2006 54(12):4077-4081

Laguri C, Stenzel RA, Donohue TJ, Phillips-Jones MK, Williamson MP
Activation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides
Biochemistry. 2006 45(25):7872-81

Williamson MP, Suzuki Y, Bourne NT, Asakura T
Binding of amyloid beta to ganglioside micelles is dependent on histidine 13
Biochem J. 2006 397(3):483-90

Williamson MP, McCormick TG, Nance CL, Shearer WT
Epigallocatechin gallate, the main polyphenol in green tea, binds to the T-cell receptor, CD4: Potential for HIV-1 therapy
J Allergy Clin Immunol. 2006 118(6):1369-74

Tunnicliffe RB, Ratcliffe EC, Hunter CN, Williamson MP
The solution structure of the PufX polypeptide from Rhodobacter sphaeroides
FEBS Letts 2006 580(30):6967-71

Williamson MP
The Nuclear Overhauser Effect
in Modern Magnetic Resonance (Ed Asakura T, Saito H, Ando I) Vol 1 Chemistry Kluwer Academic Press 2006 405-408

Williamson MP
The transferred NOE
in Modern Magnetic Resonance (Ed Craik D) Vol 2 Medical Uses Kluwer Academic Press 2006 1339-1344


2007

Moody RG, Phillips-Jones MK, Williamson MP
1H, 13C and 15N assignments for the Rhodobacter sphaeroides fasciclin 1 domain protein (Fdp)
Biomol NMR Assignments 2007 1(1):11-12

Cicortas Gunnarsson L, Montanier C, Tunnicliffe RB, Williamson MP, Gilbert HJ, Nordberg Karlsson E, Ohlin M
Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module
Biochem J. 2007 406(2):209-14

Nagy T, Tunnicliffe RB, Higgins LD, Walters C, Gilbert HJ, Williamson MP
Characterization of a double dockerin from the cellulosome of the anaerobic fungus Piromyces equi
J Mol Biol. 2007 373(3):612-22

2008

Wilton DJ, Tunnicliffe RB, Kamatari YO, Akasaka K, Williamson MP
Pressure-induced changes in the solution structure of the GB1 domain of protein G
Proteins 2008 71(3):1432-40

Bocian W, Kawecki R, Bednarek E, Sitkowski J, Williamson MP, Hansen PE, Kozerski L
Binding of topotecan to a nicked DNA oligomer in solution
Chemistry a European Journal 2008;14(9):2788-94

Wilton DJ, Ghosh M, Chary KV, Akasaka K, Williamson MP
Structural change in a B-DNA helix with hydrostatic pressure
Nucleic Acids Res. 2008 36(12):4032-7

2009

Cioffi M, Hunter CA, Packer MJ, Pandya MJ, Williamson MP
Use of quantitative 1H NMR chemical shift changes for ligand docking into barnase
J Biomol NMR. 2009 43(1):11-9

Williamson MP, Craven CJ
Automated protein structure calculation from NMR data
J Biomol NMR. 2009 43(3):131-143

Williamson MP
NOESY
in Encyclopedia of Magnetic Resonance (Ed Harris RK, Wasylishen R) John Wiley, Chichester 2009

Williamson MP
Applications of NOEs in molecular biology
Annual Reports on NMR 2009 65 Ch 3, pp 77-109

Nakazawa Y, Suzuki Y, Williamson MP, Saito H, Asakura T
The interaction of amyloid Abeta(1-40) with lipid bilayers and ganglioside as studied by 31P solid-state NMR
Chem Phys Lipids 2009 158(1):54-60

Tomlinson JH, Ullah S, Hansen PE, Williamson MP
Characterisation of salt bridges to lysines in the Protein G B1 domain
J Am Chem Soc 2009 131(13):4674-84

Wilton DJ, Kitahara R, Akasaka K, Williamson MP
Pressure-dependent 13C chemical shifts in proteins: origins and applications
J Biomol NMR 2009 44(1):25-33

Suzuki Y, Takahashi R, Shimizu T, Tansho M, Yamauchi K, Williamson MP, Asakura T
Intra- and intermolecular effects on 1H chemical shifts in a silk model peptide determined by high-field solid state 1H NMR and empirical calculations
J Phys Chem B 2009 113(29):9756-61

Wilton DJ, Kitahara R, Akasaka K, Pandya MJ, Williamson MP
Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations
Biophys J 2009 97(5):1482-90

2010

Waywell P, Thomas JA, Williamson MP
Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides
Org Biomol Chem 2010 8(3):648-654

Long J, Garner TP, Pandya MJ, Craven CJ, Chen P, Shaw B, Williamson MP, Layfield R, Searle MS
Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling
J Mol Biol 2010 396(1):178-194

Tomlinson JH, Craven CJ, Williamson MP, Pandya MJ
Dimerization of protein G B1 domain at low pH: a conformational switch caused by loss of a single hydrogen bond
Proteins: Struct Funct Bioinf 2010 78:1652-1661

Waywell P, Gonzalez V, Gill MR, Adams H, Meijer AJHM, Williamson MP, Thomas JA
Structure of the complex of [Ru(tpm)(dppz)py]2+ with a B-DNA oligonucleotide - a single-residue binding switch for a metallo-intercalator
Chem Eur J 2010 16(8):2407-2417

Giamarchi A, Feng S, Rodat-Despoix L, Xu Y, Bubenshchikova E, Newby LJ, Hao J, Gaudioso C, Crest M, Lupas AN, Honoré, Williamson MP, Obara T, Ong AC, Delmas P
A polycystin-2 dimerization domain essential for the function of heteromeric polycystin complexes
EMBO J. 2010 29(7):1176-1191

Wilson T, Williamson MP, Thomas JA
Differentiating quadruplexes: binding preferences of a luminescent dinuclear ruthenium(II) complex with four-stranded DNA structures
Org Biomol Chem 2010 8(11):2617-21

Correia MA, Abbott DW, Gloster TM, Fernandes VO, Prates JA, Montanier C, Dumon C, Williamson MP, Tunnicliffe RB, Liu Z, Flint JE, Davies GJ, Henrissat B, Coutinho PM, Fontes CM, Gilbert HJ
Signature active site architectures illuminate the molecular basis for ligand specificity in family 35 carbohydrate binding module
Biochemistry 2010 49(29):6193-205

Williamson MP, Sutcliffe MJ
Protein-protein interactions
Biochem Soc Trans 2010 38(4):875-8

Tomlinson JH, Green VL, Baker PJ, Williamson MP
Structural origins of pH-dependent chemical shifts in the B1 domain of protein G
Proteins 2010 78(14):3000-16

2011

Ratcliffe EC, Tunnicliffe RB, Ng IW, Adams PG, Qian P, Holden-Dye K, Jones MR, Williamson MP, Hunter CN
Experimental evidence that the membrane-spanning helix of PufX adopts a bent conformation that facilitates dimerisation of the Rhodobacter sphaeroides RC-LH1 complex through N-terminal interactions
Biochim Biophys Acta. 2011 1807(1):95-107

Ullah S, Ishimoto T, Williamson MP, Hansen PE
Ab initio calculations of deuterium isotope effects on chemical shifts of salt-bridged lysines
J Phys Chem B 2011 115(12):3208-3215

Trotter EW, Rolfe MD, Hounslow AM, Craven CJ, Williamson MP, Sanguinetti G, Poole RK, Green J
Reprogramming of Escherichia coli K-12 metabolism during the initial phase of transition from an anaerobic to a micro-aerobic environment
PLoS One 2011 6(9):e25501

2012

Tomlinson JH, Williamson MP
Amide temperature coefficients in the protein G B1 domain
J Biomol NMR 2012 52(1) 57-64

Asakura T, Okonogi M, Horiguchi K, Aoki A, Saitô H, Knight DP, Williamson MP
Two different packing arrangements of antiparallel polyalanine
Angewandte Chemie Int Ed 2012 51(5) 1212-1215

Williamson MP, Potts JR
Intrinsically disordered proteins: administration not executive
Biochem Soc Trans 2012 40(5) 945-949

2013

Moody RG, Williamson MP
Structure and function of a bacterial Fasciclin Domain Protein elucidates function of related cell adhesion proteins such as TGFBIp and periostin
FEBS Open Bio 2013 3 71-77

Kitazawa S, Kameda T, Yagi-Utsumi M, Sugase K, Baxter NJ, Kato K, Williamson MP, Kitahara R
Solution structure of the Q41N variant of ubiquitin as a model for the alternatively folded N2 state of ubiquitin
Biochemistry 2013 52(11) 1874-1885

Kitahara R, Hata K, Li H, Williamson MP, Akasaka K
Pressure-induced chemical shifts as probes for conformational fluctuations in proteins
Prog Nucl Magn Reson Spectrosc 2013 71 35-58

Williamson MP, Hounslow AM, Ford J, Fowler K, Hebditch M, Hansen PE
Detection of salt bridges to lysines in solution in barnase
Chem Commun 2013 49 9824-9826

Williamson MP
Using chemical shift perturbation to characterise ligand binding
Progr Nucl Magn Reson Spectrosc 2013 73 1-16

Wilson T, Costa PJ, Félix V, Williamson MP, Thomas JA
Structural studies on dinuclear ruthenium(II) complexes that bind diastereoselectively to an atiparallel folded human telomere sequence
J Med Chem 2013 56 8674-8683

2014

Kitazawa S, Kameda T, Kumo A, Yagi-Utsumi M, Baxter NJ, Kato K, Williamson MP, Kitahara R
Close identity between alternatively folded state N2 of ubiquitin and the conformation of the protein bound to the ubiquitin-activating enzyme
Biochemistry 2014 53 447-449

Mesnage S, Dellarole M, Baxter NJ, Rouget JB, Dimitrov JD, Wang N, Fujimoto Y, Hounslow AM, Lacroix-Desmazes S, Fukase K, Foster SJ, Williamson MP
Molecular basis for bacterial peptidoglycan recognition by LysM domains
Nat Commun. 2014 5:4269

Okushita K, Asano A, Williamson MP, Asakura T
Local structure and dynamics of serine in the heterogeneous structure of the crystalline domain of Bombyx mori silk fibroin in Silk II form studied by 2D 13C-13C homonuclear correlation NMR and relaxation time observation
Macromolecules 2014 47:4308-16

2015

Asakura T, Ohata T, Kametani S, Okushita K, Yazawa K, Nishiyama Y, Nishimura K, Aoki A, Suzuki F, Kaji H,  Ulrich AS and Williamson MP
Inter-molecular packing in B. mori silk fibroin: multinuclear NMR study of the model peptide (Ala-Gly)15 defines a heterogeneous antiparallel antipolar mode of assembly in the Silk II form
Macromolecules 2015 48:28-36

Asakura T, Okushita K and Williamson MP
Analysis of the structure of Bombyx mori silk fibroin by NMR
Macromolecules 2015 48:2345-2357

Xu Y, Ong ACM, Williamson MP and Hounslow AM
Backbone assignment and secondary structure of the PLAT domain of human polycystin-1
Biomolecular NMR Assignments 2015  9:369-373

Williamson MP
Pressure-dependent conformation and fluctuation in folded protein molecules
High Pressure Bioscience – Basic Concepts, Applications and Frontiers (Ed. K. Akasaka and H. Matsuki), 2015, Springer, Ch. 6, pp 109-127

2016

Xu Y, Streets AJ, Hounslow AM, Tran U, Jean-Alphonse F, Needham AJ, Vilardaga JP, Wessely O, Williamson MP and Ong ACM
The Polycystin-1, Lipoxygenase and alpha-Toxin domain regulates polycystin-1 trafficking
J Am Soc Nephrol 2016 27:1159-1173

S. Hollingshead, J. Kopečná, D. R. Armstrong, L. Bučinská, P. J. Jackson, G. E. Chen, M. J. Dickman, M. P. Williamson, R. Sobotka and C. N. Hunter
Synthesis of chlorophyll-binding proteins in a fully-segregated Delycf54 strain of the cyanobacterium Synechocystis PCC 6803
Frontiers in Plant Science 2016, 7, 292

A.E. Rawlings, J. P. Bramble, A. M. Hounslow, M. P. Williamson, A. E. Monnington, D. J. Cooke and S. S. Staniland
Ferrous iron key to Mms6 magnetite biomineralisation: A mechanistic study to understand magnetite formation using pH titration and NMR spectroscopy
Chem. Eur. J. 2016, 22, 7885-7894

Yasid NA, Rolfe MD, Green J, Williamson MP
Homeostasis of metabolites in Escherichia coli on transition from anaerobic to aerobic conditions and the transient secretion of pyruvate.
R Soc Open Sci. 2016 Aug 24;3(8):160187

J. W. Bye, N. J. Baxter, A. M. Hounslow, R. J. Falconer and M. P. Williamson
A molecular mechanism for the Hofmeister effect derived from NMR and DSC measurements on barnase
ACS Omega 2016, 1, 669-679

2017

J.D. Eaton and M.P.Williamson
Multisite binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal calorimetry
Bioscience Reports 2017, 37, BSR20170209

Blanchet P, Bebin M, Bruet S, Cooper GM, Thompson ML, Duban-Bedu B, Gerard B, Piton A, Suckno S, Deshpande C, Clowes V, Vogt J, Turnpenny P, Williamson MP, Alembik Y; Clinical Sequencing Exploratory Research Study Consortium; Deciphering Developmental Disorders Consortium, Glasgow E, McNeill A.
MYT1L mutations cause intellectual disability and variable obesity by dysregulating gene expression and development of the neuroendocrine hypothalamus.
PLoS Genet. 201713(8):e1006957

Williamson MP
The Transferred NOE
Modern Magnetic Resonance, 2nd Ed (Eds G. A. Webb and D. Craik), Springer Verlag, 2017, doi:10.1007/978-3-319-28275-6_123-1

Williamson MP
Chemical Shift Perturbation
Modern Magnetic Resonance, 2nd Ed (Eds G. A. Webb and H. Saito), Springer Verlag, 2017, doi:10.1007/978-3-319-28275-6_76-1

Heyam A, Coupland CE, Dégut C, Haley RA, Baxter NJ, Jakob L, Aguiar PM, Meister G, Williamson MP, Lagos D, Plevin MJ
Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins
Nucleic Acids Res. 2017 Oct 17. doi: 10.1093/nar/gkx928

N. J. Baxter, T. Zacharchenko, I. L. Barsukov and M. P. Williamson
Pressure-dependent chemical shifts in the R3 domain of talin show that it is thermodynamically poised for binding to either vinculin or RIAM
Structure 2017 25:1856-1866

B. K. Kudhair, A. M. Hounslow, M. D. Rolfe, J. C. Crack, D. M. Hunt, R. S. Buxton, L. J. Smith, N. E. LeBrun, M. P. Williamson and J. Green
Structure of a Wbl protein and implications for NO sensing by M. tuberculosis
Nature Communications
2017 8:2280

2018

Southam HM, Smith TW, Lyon RL, Liao C, Trevitt CR, Middlemiss LA, Cox FL, Chapman JA, El-Khamisy SF, Hippler M, Williamson MP, Henderson PJF, Poole RK
A thiol-reactive Ru(II) ion, not CO release, underlies the potent antimicrobial and cytotoxic properties of CO-releasing molecule-3
Redox Biology 2018 18:114-123









































Selected Publications

Journal articles