See also my official MBB web page

This page contains an outline of my research: the details can be found from the links

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)

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

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, 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.
From 2009-2011 I was Chair of the UK NMR discussion group, and was also (2009-2012) Chair of the Biochemical Society theme panel II (Molecular structure and function). I am a member of BBSRC Committee D (Molecules, Cells and Industrial Biotechnology) and a fellow of the Royal Society of Chemistry. From 2005-2009 I was secretary of Euromar, a group that organises annual European magnetic resonance meetings.
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.

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 three main areas:

The nuclear Overhauser effect (NOE) (link for more detail)
Chemical shifts in proteins (link for more detail)
Relaxation (link for more detail)

Carbohydrate Binding Modules (link for more detail)
These are protein modules that are used to attach degradative enzymes to their substrate, such as starch, cellulose, xylan and other cell-wall constituents. 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 (link for more detail)
This is a large membrane complex, which traps sunlighht 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 (link for more detail)
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 reviews of proline-rich regions, and a study suggesting that EGCG, the main polyphenol in green tea, may be able to slow down HIV infection.

The RegAB two-component signalling system (link for more detail)
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 showed how this works, and how the DNA is recognised.

More recently we have started work on intrinsically unstructured proteins using a variety of techniques but mainly residual dipolar couplings. Watch this space...

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.
  The paper describing the switch was featured as an inside cover in Chem. Eur. J.:
  
• a longstanding collaboration with Prof Tetsuo Asakura from the Tokyo University of Agriculture and Technology. We have worked mainly on chemical shifts, sometimes related to Prof Asakura's interest in silk. 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.
• 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 novel algorithm for calculating protein structures based on NMR data, using genetic algorithms [Protein Science 1998 7, 491-499];
• synthesis and testing of novel inhibitors/ligands for phosphoglycerate kinase [J. Med. Chem. 1998 41, 4439-4452; J. Biol. Chem., 2003, 278, 10957-10962];
• 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 collaborative study of bacterial metabolism using NMR-based metabolomics [PLoS One 2011 6(9):e25501].
• 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.
• studies on homocysteine, looking at LDL oxidation as a possible reason for its link with cardiovascular disease [BBA 2004 1688, 33-42].
• a study of polycystins 1 and 2, which are the main genetic cause of 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].
• 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 been investigating the use of deuterium isotope shifts as a way of characterising the strength of hydrogen bonds.

I have also written a number of reviews, including a recent Perspective on automated protein structure calculation and an update on NOEs in molecular biology.

I am a keen musician (when I have the time!). I play string bass and bass guitar for a jazz band. I play the cello and bass, as a member of various orchestras, and also in quartets etc. for relaxation.
I also ring bells, as a member of the band at Sheffield Cathedral, a 12-bell tower in the Yorkshire Association of Change Ringers.

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).

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 400 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

  Papers since 2001:

  2001

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  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

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  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

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  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

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  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.

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  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

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  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

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  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

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  Last updated: 16 Apr 2011 by Mike Williamson.

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