Professor Mike Williamson
School of Biosciences
Personal Chair
  
  +44 114 222 4224
Full contact details
School of Biosciences
Firth Court
Western Bank
Sheffield
S10 2TN
- Profile
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My research concentrates on protein structure and function, mainly by means of NMR, and is described in more detail below. I have written two books (The Nuclear Overhauser Effect, with David Neuhaus, 1989, second edition 2000; and How Proteins Work, Garland Science, 2011) and about 250 papers. I teach on the biochemical basis of human disease, signalling, membranes, and metabolic pathways.
I was Head of the Department of Molecular Biology and Biotechnology from 2017-2021, at which point the three biology departments merged to become the School of Biosciences. I have had many other administrative roles in the university and the department.
I was (2009-2011) Chair of the; 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); (2005-2009) secretary of ; and (2018-) a member of Council of the
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, Cambridg
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)
2017-2021 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
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During my PhD I used NMR to look at the structure and interactions of antibiotics mainly related to , 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 ).
Since then, I have worked both on NMR methodology and on determination of protein structures by NMR. In methodology, I have worked in five main areas:
The nuclear Overhauser effect (NOE)
Chemical shifts in proteins
Relaxation
Study of proteins using high pressure
Validation of protein structures in solution 
- Publications
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Show: Featured publications All publications
Featured publications
Journal articles
- . Scientific Reports, 15(1).
 - . Life, 14(5).
 - . Life, 13(4).
 - . Journal of Biomolecular NMR, 76(4), 153-163.
 - . Structure, 30(7), 925-933.e2.
 - . Structure, 29(12), 1430-1439.e2.
 - . Antioxidants, 10(6).
 - . Nature Communications, 11(-), ---.
 - . Nature Chemical Biology, 16(1), 24-30.
 - . ACS Omega, 1(4), 669-679.
 - . Nat Commun, 5, 4269.
 - . Chem Commun (Camb), 49(84), 9824-9826.
 - . Prog Nucl Magn Reson Spectrosc, 73, 1-16.
 - . Progress in Nuclear Magnetic Resonance Spectroscopy, 71, 35-58.
 - . Biophys J, 97(5), 1482-1490.
 - . Biomacromolecules, 5(3), 942-949.
 - . J Agric Food Chem, 50(6), 1593-1601.
 - The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J, 14(2), 231-241.
 - . J Biomol NMR, 9(4), 359-369.
 - . Biochem J, 297 ( Pt 2)(Pt 2), 249-260.
 - SOLUTION CONFORMATION OF PROTEINASE INHIBITOR-IIA FROM BULL SEMINAL PLASMA BY H-1 NUCLEAR MAGNETIC-RESONANCE AND DISTANCE GEOMETRY. J MOL BIOL, 182(2), 295-315.
 - STRUCTURE REVISION OF THE ANTIBIOTIC VANCOMYCIN - THE USE OF NUCLEAR OVERHAUSER EFFECT DIFFERENCE SPECTROSCOPY. J AM CHEM SOC, 103(22), 6580-6585.
 - . Redox Biology, 18, 114-123.
 
All publications
Books
- How Proteins Work. Garland Science.
 - .
 - The Nuclear Overhauser Effect in Structural and Conformational Analysis. Wiley.
 
Journal articles
- . Journal of the American Chemical Society, 147(40), 36805-36814.
 - . Scientific Reports, 15(1).
 - . Communications Biology, 8(1).
 - . Journal of Biomolecular NMR, 79(3), 155-162.
 - . Carbohydrate Polymers, 349, 122983-122983.
 - . Carbohydrate Polymers, 347.
 - . Life, 14(5).
 - . Communications Chemistry, 7(1).
 - . Journal of Biological Chemistry, 300(1).
 - . Protein Science, 32(11).
 - . International Journal of Biological Macromolecules, 245.
 - . Structure, 31(8), 975-986.e3.
 - . Life, 13(4).
 - . Saudi Journal of Biological Sciences, 30(2).
 - . PLoS ONE, 17(9).
 - . Journal of Biomolecular NMR, 76(4), 153-163.
 - . Biochemical Journal, 479(13), 1429-1439.
 - . Biomolecular NMR Assignments, 16, 247-251.
 - . Access Microbiology, 4(5).
 - . Structure, 30(7), 925-933.e2.
 - . Structure, 29(12), 1430-1439.e2.
 - . Antioxidants, 10(6).
 - . BioMed Research International, 2020, 1-17.
 - . Nature Communications, 11(-), ---.
 - . International Journal of Biological Macromolecules, 164, 3974-3983.
 - . BioMed Research International, 2020.
 - . Nature Chemical Biology, 16(1), 24-30.
 - . Scientific Reports, 9(1).
 - . Protein Science, 28(11), 1993-2003.
 - . PLoS Pathogens, 15(5).
 - . Natural Product Communications, 14(5).
 - . Journal of the American Chemical Society, 141(11), 4644-4652.
 - . Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1867(3), 350-358.
 - . Frontiers in Molecular Biosciences, 5.
 - . Nature Communications, 8(1).
 - . Structure, 25(12), 1856-1866.
 - . Nucleic Acids Research, 45(21), 12577-12584.
 - . PLoS Genetics, 13(8).
 - . Bioscience Reports, 37(3).
 - . ACS Omega, 1(4), 669-679.
 - . Royal Society Open Science, 3(8).
 - . Chemistry - A European Journal, 22(23), 7885-7894.
 - . Journal of the American Society of Nephrology, 27(4), 1159-1173.
 - . Frontiers in Plant Science, 7.
 - . Biomolecular NMR Assignments, 9(2), 369-373.
 - . Macromolecules, 48(8), 2345-2357.
 - , 109-127.
 - . Macromolecules, 48(1), 28-36.
 - . Nat Commun, 5, 4269.
 - . Macromolecules, 47(13), 4308-4316.
 - . BIOCHEMISTRY, 53(3), 447-449.
 - . Progress in Nuclear Magnetic Resonance Spectroscopy.
 - . J Med Chem, 56(21), 8674-8683.
 - . Chem Commun (Camb), 49(84), 9824-9826.
 - . Prog Nucl Magn Reson Spectrosc, 73, 1-16.
 - . Biochemistry, 52(11), 1874-1885.
 - . Progress in Nuclear Magnetic Resonance Spectroscopy, 71, 35-58.
 - . FEBS Open Bio, 3, 71-77.
 - . Seibutsu Butsuri, 53(supplement1-2), S160-S160.
 - . Biochem Soc Trans, 40(5), 945-949.
 - . Nature Structural & Molecular Biology, 19(9), 854-860.
 - . Seibutsu Butsuri, 52(supplement), S87-S87.
 - . Angewandte Chemie, 124(5), 1238-1241.
 - . ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 51(5), 1212-1215.
 - . J Biomol NMR, 52(1), 57-64.
 - . Plos One, 6(9).
 - . ChemInform, 42(18).
 - . J PHYS CHEM B, 115(12), 3208-3215.
 - Amide temperature coefficients in the protein G B1 domain. Journal of Biomolecular NMR, 1-8.
 - . Biochim Biophys Acta, 1807(1), 95-107.
 - . Proteins, 78(14), 3000-3016.
 - . Biochem Soc Trans, 38(4), 875-878.
 - . BIOCHEMISTRY-US, 49(29), 6193-6205.
 - . Org Biomol Chem, 8(11), 2617-2621.
 - . EMBO J, 29(7), 1176-1191.
 - . Chemistry – A European Journal, 16(8), 2324-2324.
 - . Chemistry, 16(8), 2407-2417.
 - . Proteins, 78(7), 1652-1661.
 - . Org Biomol Chem, 8(3), 648-654.
 - . J MOL BIOL, 396(1), 178-194.
 - . Biophys J, 97(5), 1482-1490.
 - . J PHYS CHEM B, 113(29), 9756-9761.
 - . J Biomol NMR, 44(1), 25-33.
 - . J Am Chem Soc, 131(13), 4674-4684.
 - . J Biomol NMR, 43(3), 131-143.
 - . CHEM PHYS LIPIDS, 158(1), 54-60.
 - . J Biomol NMR, 43(1), 11-19.
 - . Nucleic Acids Res, 36(12), 4032-4037.
 - . CHEM-EUR J, 14(9), 2788-2794.
 - . Proteins, 71(3), 1432-1440.
 - . J MOL BIOL, 373(3), 612-622.
 - . Biochemical Journal, 406(2), 209-214.
 - . BIOMOL NMR ASSIGM, 1(1), 11-12.
 - . FEBS Lett, 580(30), 6967-6971.
 - . J Allergy Clin Immunol, 118(6), 1369-1374.
 - . Biochem J, 397(3), 483-490.
 - . Biochemistry, 45(25), 7872-7881.
 - . J Agric Food Chem, 54(12), 4077-4081.
 - . FEBS LETT, 580(13), 3206-3210.
 - . Mol Microbiol, 60(5), 1262-1275.
 - . Structure, 13(11), 1677-1684.
 - . J Agric Food Chem, 53(20), 7997-8002.
 - . Biochem Soc Trans, 33(Pt 3), 503-506.
 - . Journal of Experimental Medicine , 201(10), 1637-1645.
 - . J Mol Biol, 347(2), 287-296.
 - . J BIOL CHEM, 280(25), 23718-23726.
 - . CHEM-EUR J, 10(22), 5776-5787.
 - . Biomacromolecules, 5(3), 942-949.
 - . Journal of Allergy and Clinical Immunology, 113(2), S256-S256.
 - . Biochim Biophys Acta, 1688(1), 33-42.
 - . BIOCATAL BIOTRANSFOR, 21(4-5), 253-260.
 - . Protein Sci, 12(9), 1971-1979.
 - . Nucleic Acids Res, 31(23), 6778-6787.
 - . Proteins, 53(3), 731-739.
 - . Biochemistry, 42(31), 9316-9323.
 - . J Mol Biol, 327(4), 857-865.
 - . Seibutsu Butsuri, 43(supplement), S7-S7.
 - . J Biol Chem, 278(13), 10957-10962.
 - . Biochemistry, 42(2), 257-264.
 - . J Am Chem Soc, 124(33), 9899-9905.
 - . BIOCHEMISTRY-US, 41(18), 5720-5729.
 - . Biochemistry, 41(18), 5712-5719.
 - Letter to the Editor: Virtually complete H-1, C-13 and N-15 resonance assignments of the second family 4 xylan binding module of Rhodothermus marinus xylanase 10A. J BIOMOL NMR, 22(2), 187-188.
 - . J Agric Food Chem, 50(6), 1593-1601.
 - . J MOL BIOL, 320(2), 201-213.
 - Chemical dreams. CHEM BRIT, 38(1), 19-19.
 - . Nat Struct Biol, 8(9), 775-778.
 - . BIOCHEMISTRY-US, 40(31), 9167-9176.
 - . Microbiology (Reading), 147(Pt 6), 1473-1482.
 - . BIOCHEMISTRY-US, 40(19), 5700-5707.
 - Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR. J BIOMOL NMR, 19(2), 115-124.
 - A nicked duplex decamer DNA with a PEG(6) tether. NUCLEIC ACIDS RES, 29(5), 1132-1143.
 - Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A. BIOCHEMISTRY-US, 40(8), 2468-2477.
 - Structure determination of [Arg8]vasopressin methylenedithioether in dimethylsulfoxide using NMR. EUR J BIOCHEM, 267(14), 4504-4510.
 - . J Biol Chem, 275(52), 41137-41142.
 - Structure and dynamics of photosynthetic membrane-bound proteins in Rhodobacter Sphaeroides, studied with solid-state NMR spectroscopy. PHOTOSYNTH RES, 63(3), 259-267.
 - . J Mol Biol, 298(1), 83-94.
 - The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J, 14(2), 231-241.
 - Trp22, Trp24, and Tyr8 play a pivotal role in the binding of the family 10 cellulose-binding module from Pseudomonas xylanase A to insoluble ligands. BIOCHEMISTRY-US, 39(5), 985-991.
 - . Biochemistry, 39(5), 978-984.
 - An advantage for use of isotope labeling and NMR chemical shifts to analyze the structure of four homologous IgG-binding domains of staphylococcal protein A. J BIOCHEM BIOPH METH, 42(1-2), 35-47.
 - The self-association of the black tea polyphenol theaflavin and its complexation with caffeine. J CHEM SOC PERK T 2(2), 317-322.
 - . Biochemical Journal, 345(1), 53-53.
 - Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase: cloning, expression and binding studies. BIOCHEM J, 345, 53-60.
 - Highly potent bisphosphonate ligands for phosphoglycerate kinase and protein binding studies. PHOSPHORUS SULFUR AND SILICON AND THE RELATED ELEMENTS, 146, 533-536.
 - . Biochemical Journal, 342(2), 473-473.
 - The type II and X cellulose-binding domains of Pseudomonas xylanase A potentiate catalytic activity against complex substrates by a common mechanism. BIOCHEM J, 342, 473-480.
 - . Structure, 7(7), 853-864.
 - Solid phase synthesis and biological activities of [Arg(8)]-vasopressin methylenedithioether. BIOORG MED CHEM LETT, 9(13), 1767-1772.
 - . J Bacteriol, 181(13), 3956-3966.
 - C-alpha and C-beta carbon-13 chemical shifts in proteins from an empirical database. J BIOMOL NMR, 13(3), 199-211.
 - . FEBS Lett, 447(1), 58-60.
 - A light-harvesting antenna protein retains its folded conformation in the absence of protein-lipid and protein-pigment interactions. BIOPOLYMERS, 49(5), 361-372.
 - Stereochemical model of [2+2]cycloaddition of chlorosulfonyl isocyanate to chiral vinyl ethers. J CHEM SOC PERK T 2(2), 217-224.
 - . Protein Sci, 7(2), 491-499.
 - The structure of the melittin tetramer at different temperatures - An NOE-based calculation with chemical shift refinement. EUR J BIOCHEM, 257(2), 479-487.
 - . J Mol Biol, 284(5), 1625-1639.
 - . J Med Chem, 41(23), 4439-4452.
 - . Bioorg Med Chem Lett, 8(18), 2603-2608.
 - . J Bacteriol, 180(17), 4603-4612.
 - All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands. FEBS LETT, 429(3), 312-316.
 - Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity. BIOCHEM J, 331, 775-781.
 - . ChemInform, 28(51).
 - Structure and conformation of the procyanidin B-2 dimer. MAGN RESON CHEM, 35(12), 854-858.
 - NMR study of silk I structure of Bombyx mori silk fibroin with N-15- and C-13-NMR chemical shift contour plots. BIOPOLYMERS, 41(2), 193-203.
 - . Methods Mol Biol, 60, 53-69.
 - . Biochemistry, 36(24), 7535-7539.
 - . Pharm Res, 14(5), 625-630.
 - . Biochemistry, 36(18), 5566-5577.
 - Towards stereochemical and conformational assignment in flexible molecules using NOEs and molecular modelling. J CHEM SOC PERK T 2(9), 1811-1818.
 - . J Biomol NMR, 9(4), 359-369.
 - . J Biomol NMR, 9(4), 389-395.
 - Protein chemical shifts., 60, 53-69.
 - . Structure, 5(5), 647-661.
 - . FEBS Lett, 382(3), 289-292.
 - Human cytochrome P450 3A4 is involved in the biotransformation of the herbicide 2,4-dichlorophenoxyacetic acid. ENVIRON TOXICOL PHAR, 2(4), 397-401.
 - . J Mol Biol, 259(5), 970-987.
 - Stacking interactions between caffeine and methyl gallate. J CHEM SOC FARADAY T, 92(2), 231-234.
 - Synthesis and kinetic studies of bisubstrate analogues of phosphoglycerate kinase. COLLECTION OF CZECHOSLOVAK CHEMICAL COMMUNICATIONS, 61, S88-S91.
 - . Chemosphere, 33(4), 759-769.
 - . Eur J Biochem, 233(2), 568-578.
 - . Eur J Biochem, 233(2), 561-567.
 - SEARCHING CONFORMATIONAL SPACE IN FLEXIBLE MOLECULES USING NOES AND MOLECULAR MODELING. J ORG CHEM, 60(11), 3533-3538.
 - . J Mol Biol, 247(4), 541-546.
 - THE RELATIONSHIP BETWEEN AMIDE PROTON CHEMICAL-SHIFTS AND SECONDARY STRUCTURE IN PROTEINS. J BIOMOL NMR, 6(3), 227-236.
 - NMR-STUDIES OF DEXTRAN OLIGOMER INTERACTIONS WITH MODEL POLYPHENOLS. CARBOHYD RES, 266(2), 229-235.
 - . Eur J Biochem, 219(3), 923-935.
 - . Eur J Biochem, 219(3), 915-921.
 - SYNTHESIS OF PHOSPHONATE ANALOGS OF 1,3-BISPHOSPHOGLYCERIC ACID AND THEIR BINDING TO YEAST PHOSPHOGLYCERATE KINASE. BIOORG MED CHEM LETT, 4(21), 2573-2578.
 - . Biochem J, 303 ( Pt 1)(Pt 1), 303-311.
 - . Biochem Soc Trans, 22(1), 140-144.
 - . Biochem J, 297 ( Pt 2)(Pt 2), 249-260.
 - STRUCTURE-ANALYSIS OF PROTEINS BY A COMBINATION OF DISTANCE GEOMETRY CALCULATION AND H-1-NMR CHEMICAL-SHIFT CALCULATION. KOBUNSHI RONBUNSHU, 51(6), 409-413.
 - . Phytochemistry, 37(2), 357-371.
 - . ChemInform, 24(12).
 - . FEBS Lett, 323(3), 243-246.
 - . Nat Prod Rep, 10(3), 207-232.
 - TURGOR REGULATION IN A NOVEL HALOMONAS SPECIES. ARCH MICROBIOL, 160(4), 319-323.
 - . Methods Mol Biol, 17, 69-85.
 - . Protein Eng, 6(1), 101-108.
 - EMPIRICAL COMPARISONS OF MODELS FOR CHEMICAL-SHIFT CALCULATION IN PROTEINS. J MAGN RESON SER B, 101(1), 63-71.
 - . Collection of Czechoslovak Chemical Communications, 58(s1), 109-112.
 - O-GLYCOSYLATION AND STABILITY - UNFOLDING OF GLUCOAMYLASE INDUCED BY HEAT AND GUANIDINE-HYDROCHLORIDE. EUR J BIOCHEM, 207(2), 661-670.
 - . FEBS Lett, 302(2), 185-188.
 - PEPTIDE STRUCTURE FROM NMR. CHEM SOC REV, 21(4), 227-236.
 - . Biochem Biophys Res Commun, 189(1), 414-423.
 - O-GLYCOSYLATION IN ASPERGILLUS GLUCOAMYLASE - CONFORMATION AND ROLE IN BINDING. BIOCHEM J, 282, 423-428.
 - DETERMINATION OF THE MAGNETIC-ANISOTROPY OF THE OXYGEN ATOM AND H-1 CHEMICAL-SHIFT CALCULATION OF PROTEINS. J MAGN RESON, 98(3), 646-653.
 - IMPROVED EXPERIMENTS FOR THE ASSIGNMENT OF CROWDED PEPTIDE SPECTRA. J MAGN RESON, 100(3), 593-597.
 - . J Biomol NMR, 2(1), 83-98.
 - . ChemInform, 22(32).
 - . Journal of Molecular Biology, 221(4), 1269-1293.
 - CALCULATION OF CHEMICAL-SHIFTS OF PROTONS ON ALPHA CARBONS IN PROTEINS. J MAGN RESON, 94(3), 557-562.
 - NMR IN PROTEIN STUDIES. CHEM BRIT, 27(4), 335-337.
 - . Journal of the Chemical Society Perkin Transactions 2(5), 601-606.
 - . Biopolymers, 29(10-11), 1423-1431.
 - . Biochemistry, 29(12), 2895-2905.
 - . Journal of Magnetic Resonance 1969, 88(1), 177-185.
 - SECONDARY-STRUCTURE DEPENDENT CHEMICAL-SHIFTS IN PROTEINS. BIOPOLYMERS, 29(10-11), 1428-1431.
 - . FEBS Letters, 254(1-2), 171-173.
 - . Biochim Biophys Acta, 997(1-2), 9-14.
 - . J Mol Biol, 206(2), 407-410.
 - . Br J Rheumatol, 28(1), 23-27.
 - H-1 NUCLEAR MAGNETIC-RESONANCE INVESTIGATION OF SYNOVIAL-FLUID COMPONENTS IN OSTEO-ARTHRITIS, RHEUMATOID-ARTHRITIS AND TRAUMATIC EFFUSIONS. BRIT J RHEUMATOL, 28(1), 23-27.
 - . ChemInform, 19(44).
 - STRUCTURE ELUCIDATION OF A GLYCOPEPTIDE ANTIBIOTIC, OA-7653. J CHEM SOC PERK T 1(7), 1949-1956.
 - . ChemInform, 18(45).
 - . MAGNETIC RESONANCE IN CHEMISTRY, 25(4), 356-361.
 - THE NUCLEAR OVERHAUSER EFFECT IN STRONGLY COUPLED SPIN SYSTEMS. J MAGN RESON, 73(1), 45-68.
 - SYMMETRY IN NOE SPECTRA. J MAGN RESON, 72(2), 369-375.
 - . European Journal of Biochemistry, 158(3), 527-536.
 - SECONDARY STRUCTURE OF A HERPES-SIMPLEX VIRUS GLYCOPROTEIN-D ANTIGENIC DOMAIN. INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH, 27(5), 562-568.
 - 1 H N.M.R. Studies of the structure of ristocetin a and of its complexes with bacterial cell wall analogues in aqueous solution. Journal of the Chemical Society, Perkin Transactions 1, 949-956.
 - SOLUTION CONFORMATION OF PROTEINASE INHIBITOR-IIA FROM BULL SEMINAL PLASMA BY H-1 NUCLEAR MAGNETIC-RESONANCE AND DISTANCE GEOMETRY. J MOL BIOL, 182(2), 295-315.
 - H-1-NMR STUDIES OF THE STRUCTURE OF RISTOCETIN-A AND OF ITS COMPLEXES WITH BACTERIAL-CELL WALL ANALOGS IN AQUEOUS-SOLUTION. J CHEM SOC PERK T 1(5), 949-956.
 - STRUCTURAL FEATURES THAT AFFECT THE BINDING OF TEICOPLANIN, RISTOCETIN-A, AND THEIR DERIVATIVES TO THE BACTERIAL CELL-WALL MODEL N-ACETYL-D-ALANYL-D-ALANINE. J CHEM SOC CHEM COMM(5), 254-256.
 - HYDROPHOBIC INTERACTIONS AFFECT HYDROGEN-BOND STRENGTHS IN COMPLEXES BETWEEN PEPTIDES AND VANCOMYCIN OR RISTOCETIN. EUR J BIOCHEM, 138(2), 345-348.
 - A GLOBULAR PROTEIN WITH SLOWER AMIDE PROTON-EXCHANGE FROM AN ALPHA-HELIX THAN FROM ANTIPARALLEL BETA-SHEETS. BIOCHEM BIOPH RES CO, 122(3), 1174-1178.
 - SECONDARY STRUCTURE IN THE SOLUTION CONFORMATION OF THE PROTEINASE INHIBITOR-IIA FROM BULL SEMINAL PLASMA BY NUCLEAR MAGNETIC-RESONANCE. J MOL BIOL, 173(3), 341-359.
 - INTERACTIONS OF VANCOMYCIN AND RISTOCETIN WITH PEPTIDES AS A MODEL FOR PROTEIN-BINDING. TETRAHEDRON, 40(3), 569-577.
 - DETAILED BINDING-SITES OF THE ANTIBIOTICS VANCOMYCIN AND RISTOCETIN-A - DETERMINATION OF INTERMOLECULAR DISTANCES IN ANTIBIOTIC SUBSTRATE COMPLEXES BY USE OF THE TIME-DEPENDENT NOE. J AM CHEM SOC, 105(5), 1332-1339.
 - PURE ABSORPTION PHASE PROTON 2D J-RESOLVED SPECTROSCOPY. J MAGN RESON, 55(3), 471-474.
 - STRUCTURE AND CONFORMATION OF 14 ANTIBIOTICS OF THE QUINOXALINE GROUP DETERMINED BY H-1-NMR. J ANTIBIOT, 35(1), 62-66.
 - ON THE BIOSYNTHESIS OF THE ANTIBIOTIC VANCOMYCIN. J CHEM SOC CHEM COMM(6), 344-346.
 - STRUCTURE REVISION OF THE ANTIBIOTIC VANCOMYCIN - THE USE OF NUCLEAR OVERHAUSER EFFECT DIFFERENCE SPECTROSCOPY. J AM CHEM SOC, 103(22), 6580-6585.
 - Erratum: Manipulation of the nuclear overhauser effect by the use of a viscous solvent: The solution conformation of the antibiotic echinomycin (Journal of the Chemical Society, Chemical Communications (1981) (165)). Journal of the Chemical Society Chemical Communications(9), 440.
 - A C-13 NUCLEAR MAGNETIC-RESONANCE STUDY OF RISTOCETIN-A AND RISTOCETIN-B AND THEIR DERIVATIVES. J CHEM SOC PERK T 1(5), 1483-1491.
 - MANIPULATION OF THE NUCLEAR OVERHAUSER EFFECT BY THE USE OF A VISCOUS SOLVENT - THE SOLUTION CONFORMATION OF THE ANTIBIOTIC ECHINOMYCIN. J CHEM SOC CHEM COMM(4), 165-166.
 - ASSIGNMENT OF THE C-13 SPECTRUM OF VANCOMYCIN AND ITS DERIVATIVES. J CHEM SOC PERK T 2(1), 201-206.
 - A C-13 NMR-STUDY OF THE CARBOHYDRATE PORTION OF RISTOCETIN-A. TETRAHEDRON LETT, 21(43), 4187-4188.
 - STRUCTURE OF THE ANTIBIOTIC RISTOCETIN-A. J CHEM SOC CHEM COMM(20), 906-908.
 - . Redox Biology, 18, 114-123.
 
Book chapters
- , Encyclopedia of Analytical Science (pp. 264-271).
 - , Modern Magnetic Resonance (pp. 2133-2147). Springer International Publishing
 - , Modern Magnetic Resonance (pp. 995-1012). Springer International Publishing
 - , Reference Module in Chemistry, Molecular Sciences and Chemical Engineering Elsevier
 - , Modern Magnetic Resonance (pp. 1-15). Springer International Publishing
 - , Modern Magnetic Resonance (pp. 1-19). Springer International Publishing
 - , Encyclopedia of Analytical Science (pp. V6-V6-349).
 - , Encyclopedia of Analytical Science (pp. 342-349). Elsevier
 - , Phytochemicals in Human Health Protection, Nutrition, and Plant Defense (pp. 289-318). Springer US
 - , World Scientific Series in 20th Century Chemistry (pp. 319-339). WORLD SCIENTIFIC
 - John Wiley & Sons, Ltd
 - , Modern Magnetic Resonance (pp. 409-412). Springer Netherlands
 - , Modern Magnetic Resonance (pp. 1357-1362). Springer Netherlands
 - John Wiley & Sons, Ltd
 
Conference proceedings
- Epigallocatechin gallate, green tea catechin, binds to the T cell receptor, CD4. JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, Vol. 117(2) (pp S325-S325)
 - 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)
 - Structural and dynamical studies of Aβ(1-40)-Ganglioside system with solid state and solution NMR. Polymer Preprints Japan, Vol. 54(1) (pp 727)
 - 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)
 - . MAGNETIC RESONANCE IN CHEMISTRY, Vol. 41 (pp S64-S69)
 - Protein-polyphenol interactions. International Congress and Symposium Series Royal Society of Medicine(226) (pp 25-33)
 - How the N-terminal xylan-binding domain from C-fimi xylanase D recognises xylan. RECENT ADVANCES IN CARBOHYDRATE BIOENGINEERING(246) (pp 212-220)
 - Structural analysis of silk with C-13 NMR chemical shift contour plots. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, Vol. 24(2-3) (pp 167-171)
 - Salivary proteins as a defence against dietary tannins. COST 916 - POLYPHENOLS IN FOOD (pp 179-185)
 - Salivary proline-rich proteins as a defence against dietary tannins. COST 916 - POLYPHENOLS IN FOOD (pp 201-201)
 - AN ENZYME AND C-13-NMR STUDY OF CARBON METABOLISM IN HELIOBACTERIA. PHOTOSYNTHESIS RESEARCH, Vol. 41(1) (pp 75-88)
 - . [1990] Proceedings of the Twelfth Annual International Conference of the IEEE Engineering in Medicine and Biology Society (pp 1612-1612)
 
Preprints
- , Cold Spring Harbor Laboratory.
 - , Springer Science and Business Media LLC.
 - , Cold Spring Harbor Laboratory.
 - , Cold Spring Harbor Laboratory.
 - , Cold Spring Harbor Laboratory.
 - , Cold Spring Harbor Laboratory.
 
 
- Research group
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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
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Projects and literature reviews at levels 3 and 4, and tutorial groups.
Level 3 modules
Biochemical Basis of Human Disease (module coordinator) - amyloid disease, obesity, inflammation and diabetes
Biochemical Signalling - principles, receptor tyrosine kinases, Notch and NF-kB
Protein folding and misfolding in disease
Level 2 modules
Biostructures, Energetics and Synthesis – biochemical pathways, membranes, nerve transmission and signalling
Ethics and Philosophy for Molecular Biosciences 
- Professional activities and memberships
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Council of International Conference for Magnetic Resonance in Biological Systems (ICMRBS) since 2018.
Reviewing grant applications, papers, promotion cases.
Editorial board of Biomolecules. 
Links