Oxford University Biomembrane Structure Unit

Oxford University Biomembrane Structure Unit (OUBSU), directed by Professor Anthony Watts, has its main labs
in the Department of Biochemistry at Oxford. The Unit's solid state nuclear magnetic resonance (NMR) labs are at the Biological Solid State NMR Facility, at the STFC's Rutherford
Appleton Laboratory near Didcot.


The main research interests of the Watts's group focus on the study of the structure of small molecules when at their site of action in membrane-bound proteins whilst in their native, fully functional form in membranes. In addition,
peptides which form channels in membranes are being studied to high resolution using solid state NMR methods. The potential for understanding how the membrane-bound targets for hormones, solutes and drugs function can be realised
with this emerging technology.


The NMR Facility was opened in 1998, funded through investments by HEFCE and UK Research Councils with matching funds from instrument manufacturers. It is equipped as one of the major
solid state biological NMR centres in the world and now has some of the most advanced instruments (at 200MHz, 400MHz, 500MHz and 800MHz) and support facilities anywhere world-wide for use in structural biology.


The Watts lab traveled to Portugal for the Bionanotechnology meeting in Sesimbra from 10-13 July and the EBSA Congress in Lisbon 13-17 July, 2013. Here are some pictures of the events.





Over the last 20 years, a large battery of methods and techniques has been applied to the study of biomembranes, accumulated through unbroken, significant funding from a range of national and international sources. In particular, a new approach to membrane studies has been developed, namely the exploitation of solid state NMR to resolve both dynamics and structural details of membrane proteins and lipids.


The group conducts research in 3 principal fields, although there is often overlap between disciplines:


  • Membrane protein structure
  • Bionanotechnology
  • Drug target interactions

    Membrane Protein Structure

    Through the use of wide-line, solid state NMR, the perturbation of bilayer surfaces induced by integral and peripheral proteins has been studied. In this context, the "molten globule" state of a membrane associated protein, cytochrome c, has been identified. These studies are being complemented with stopped-flow fluorescence and CD studies of the insertion, folding and translocation of apocytochrome c and cytochrome c, into anionic lipid bilayers. For this work, cardiolipin, synthesized using a new route resolved by us, is being employed.

    This structural work on integral membrane proteins requires instrumental development (coils, probes, computational analysis) as well as bio-organic chemistry (synthesis of isotopically enriched molecules), membrane biochemistry (isolation, purification and functional description of proteins) and molecular biology (expression of proteins). The potential for the method is significant and, in the absence of other approaches, may be the only method by which the pertinent details of membrane proteins, and their regions involved in defining molecular specificity, may be described in detail for some time to come.

    Using both static and magic angle solid state NMR methods, we have been resolving structural details of large, fully functional integral membrane proteins in natural and reconstituted membranes. These methods permit atomic details to be obtained of well-defined regions of integral membrane proteins, namely those regions associated with ligand or prosthetic group binding, which may be intractable by crystallographic or other spectroscopic methods. Indeed, in the absence of routine crystallography, it is likely that structure-function relationships of membrane proteins can be described at the molecular level only through the use of such alternative methods. Proteins currently under study are bacteriorhodopsin, the gastric H+/K+-ATPase, the kidney Na+/K+-ATPase, the over-expressed GalP sugar transporter,nicotinic acetylcholine receptor, phospholamban and vertebrate and invertebrate rhodopsin.

    In bacteriorhodopsin, we have been able to define the conformation and orientation of retinal whilst within the protein binding site and in the membrane using NMR observation of deuterated retinal using an ab initio approach. Curvature of the retinal polyene chain has been defined for the first time, as well as the known orientation of the ß-ionone ring of the retinal with respect to the protein. Much, but not all, experimental information available for this protein is confirmed by this non-perturbing NMR approach. Also the lack of any large change in retinal orientation within the protein during the photocycle observed using this non-perturbing approach, is already helping to redefine descriptions of the proton gradient generation by the protein on photon incidence.

    Membrane protein function is controlled and regulated by, amongst other factors, the local lipid environment. Lipid-protein interactions have been studied and classes of lipids described which either have non-specific, solubilizing function, a specific functional role or combination of the two rôles. Spin-label ESR and deuterium NMR methods have both been used to prove, since it was very contentious at one time, that both spectroscopic methods can give consistent views of lipid-protein interaction and the molecular specificity of such interaction. Some fifteen proteins have been studied by various groups and we have been involved with about one third of this number. The wealth of information obtained has required much bio-organic chemistry (spin-label and deuterated lipid synthesis) and membrane protein functional reconstitution technology.

    More recently, lipid-protein interactions have been found to be important in producing and stabilizing 2D-arrays of integral proteins in membranes. One particular lipid, phosphatidylglycerol phosphate is essential (and the sulphate derivative less so) in the formation of 2D arrays of bacteriorhodopsin. This has been shown by electron microscopic methods and by controlled reconstitution methods and the enigma of why and how this protein forms arrays is now resolved. Other proteins are now being examined with a view to producing routine 2D arrays for structural work.

    Multidisciplinary approaches to the study of membrane structure and function are therefore used in all aspects of the current work. Most biophysical methods have been used including NMR, ESR, ultracentrifugation, diffraction (X-ray, optical and neutron), differential scanning calorimetry, electron microscopy, CD and computational approaches. The general approach is thus to address a system and a problem with a range of appropriate methods, rather than specialize in one method. All this work has been, and is being funded through significant BBSRC/HSFP, EC and MRC programme grants as well as project grant support from BBSRC, EPSRC and MRC.



    Since ~50-85% of all drug targets for the next decade are membrane-bound proteins, this important class of biological macromolecule lends itself to non-native uses as sensors, detectors and control devices.

    Photoreceptor proteins can be used as light detectors and nanometer-scale photoswitches.

    Small molecule-activated receptors can be employed to detect small molecules such as hormones or drugs and can act as signal amplifiers.

    Membrane proteins have many bionanotechnological advantages, including: (sub)-nanometer scale, single molecule application, very high chemical and biological specificity, fast response times, and exceptionally high efficiency.

    We are investigating the functional mechanism of these membrane proteins, modulation with small molecule modulators and protein­lipid interactions on an atomic level. These studies serve as a basis for the design of novel functional units and membrane proteins with new functions. A series of techniques such as NMR spectroscopy, molecular dynamics simulations, and bilayer recordings, supported by solid phase peptide synthesis and expression is used in our laboratories. The projects are supported by the Bionanotechnology IRC which is based on funding from the BBSRC.


    Drug Target Interactions

    Solid state NMR used as major tool in drug structure determination to sub-nanometer (± 0.03nm) resolution. Drug ligands, such as substituted imidazopyridines in peptic ulcer treatment, acetylcholine in neurological disease treatment (Schizophrenia), and brain neurotensin in treatment of Parkinson's, are all being examined using solid state NMR technology.

    Atomic force microscopy (AFM) is being used to visualize conformational changes in membrane receptors upon activation by their ligands. Force measurements made using AFM provide information about binding energies and the selectivity of the ligand - informing the process of rational drug design.


    Our research entered a new phase with the sucessful installation of a Magnex 800MHz wide bore (89mm) magnet at the beginning of January 2004. This machine is the largest worldwide for solid state biological work and complements the existing machines in
    the Facility.

    Currently the Facility has 2- and 3-channel NMR spectrometers with wide bore (89mm) magnets operating at 1H frequencies at 200, 400, 500 and
    800MHz (Varian, Inc., Bruker, Magnex, Oxford Instruments).

    There are also computational facilities (SGIs, O2, and Octanes) and a biochemical preparation laboratory (Beckman, Tektronix, BoroLabs). Research projects are supported by BBSRC, MRC, EPSRC, EU and HEFCE.


    Solid State NMR Magnets

    The Oxford University Biomembrane Structure Unit currently has four magnets located in R34 at the Rutherford Appleton Laboratories, Harwell.

    All magnets are wide-bore (89mm bore diameter) and have a range of probes to suit the fields. We currently have probes suitable for static (non-spinning) work and for magic-angle spinning studies. Rotor sizes vary from 2.5 - 7mm diameter. The probes
    are single-. double-, or triple-channeled, including a 4mm 1H19FX probe from Varian, Inc.

    Experiment acquisition is supported by consoles from Chemagnetics, Varian, and Bruker. Our most recent magnet and console installation was in January 2005 when a new 500/89 shielded Magnex magnet was installed together with a Varian Infinity+ console.


    Oxford Instruments 400 MHz:

    The 400 MHz wide-bore Oxford Instruments magnet is supported by a 3-channel CMX Infinity spectrometer (1H 1 kW and 2 broadband 1 kW amplifiers).

    Bruker 400 MHz:

    Spectrospin wide-bore magnet is supported by a Bruker Avance 400 spectrometer (1H 1 kW and 2 broadband 1 kW amplifiers).

    Magnex 500 MHz (Infinity+):

    The 500 MHz wide-bore Magnex magnet is shielded and is supported by a 3-channel Varian Infinity+ spectrometer (1H 1 kW and 2 broadband 1 kW amplifiers).Probe base:

  • Varian 4mm HX MAS
  • Varian 4mm HFX MAS
  • Varian 6mm HXY MAS
  • Varian X Static
  • Magnex 800 MHz (Infinity+):

    The 800 MHz wide-bore Magnex magnet is unshielded and is supported by a 3-channel Varian Infinity+ spectrometer (1H 1 kW and 2 broadband 1 kW amplifiers).Probe base:

  • Varian 2.5mm HX MAS
  • Varian 3.2mm HX MAS
  • Varian 4mm HXY MAS
  • DOTY 5mm HX MAS
  • OUBSU Publications : since 2005

    Citation metrics (1972-2018)

    Publications - 2018

    • P. Dijkman, O. Castell , A. Goddard , J. Munoz-Garcia , C. de Graaf , M. Wallace and A. Watts (2018) Dynamic tuneable G protein-coupled receptor monomer-dimer populations, Nature Comms
    • C. Sun, X. Ding, H. Cui, Y. Yang, S. Chen, A. Watts and X. Zhao (2018) "In situ study of the functions of bacterioruberin in the dual-chromophore photoreceptor, archaerhodopsin-4",Angew. Chemie. (Intl). (in press)
    • J. C. Muñoz-García[, R. I. dos Reis , R. J. Taylor, A. J. Henry and A. Watts (2018)"Nanodisc-Targeted STD NMR Spectroscopy Reveals Atomic Details of Ligand Binding to Lipid Environments" ChemBioChem.
    • M-P. Pfeil, A. Pyne, V. Losasso, J. Ravi, B. Lamarre, N. Faruqui, H. Alkassem, K. Hammond, P. Judge, M. Winn, G. Martyna, J. Crain, A. Watts, B. Hoogenboom, and M. Ryadnov (2018) "Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms" Sci. Reports (under revision)
    • X. Ding, C. Sun, H. Cui, S. Chen, Y. Gao, Y. Yang, J. Wang, X. He, D. Iuga, F. Tian, A. Watts and X. Zhao (2018) Functional roles of tyrosine 185 during the bacteriorhodopsin photocycle revealed by in-situ spectroscopic studies. BBA Biomembranes, (in press)

    Publications - 2017

    Publications - 2016

    Publications - 2015











    • Kamihira, M., Vosegaard, T., Mason, A.J., Straus, S.K., Nielsen, N.C. & Watts, A. (2005) Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy. J. Struct. Biol., 149, 7-16.
    • Lemaitre, V., Yeagle, P. & Watts, A. (2005) Molecular dynamic simulations of retinal in rhodopsin: from the dark-adapted state towards lumirhodopsin. Biochemistry, 44, 12667-12680. (Suppl. Info.).
    • Kim, C.G., Watts, J.A. & Watts, A. (2005) Ligand docking in the gastric H+/K+-ATPase - homology modelling of reversible inhibitor binding sites. J. Med Chem. 48, 7145-7152.
    • Contera, S.A., Lemaitre, V., de Planque, M.R.R., Watts, A. & Ryan, J.F. (2005) Unfolding and extraction of an a-helical peptide from a lipid bilayer: Dynamic Force Spectroscopy and Molecular Dynamics. Biophys J. 89, 3129-3140.
    • Candler, A., Featherstone, M. Ali, R., Maloney, L., Watts A. & Fischer, W.B. (2005) Computational analysis of mutations in the transmembrane region of Vpu from HIV-1. Biochim. Biophys. Acta, 1716, 1-10.
    • Williamson, P.T.F., Zandomeneghi, G., Barrantes, F.J., Watts, A. & Meier, B.H. (2005) Structural and dynamic studies of the g-M4 trans-membrane domain of the nicotinic acetylcholine receptor. Mol. Membrane Biol., 22, 485-496.
    • Watts, A. (2005) Solid state NMR in drug design and discovery for membrane embedded targets. Nature Reviews Drug Discovery, 4, 555-568.
    • Lemaître, V., Kim, C.G., Lam, Y.-H., Fischer, D., Watts, A. & Fischer, W.B. (2005) Defining drug-protein interactions of Vpu MD simulations and drug-protein interactions. In: Protein Reviews: Viral membrane proteins: Structure, function and drug design , (Ed. W. B. Fischer, Series Editor Z. Atassi), Kluwer Academikc/Plenum Publishers, New York, Ch. 14, 187-200.

    Citation Metrics (1972-2017)

    Cited peer-reviewed publications

    Total citations*


    Tapered h-Index[2]*





    Total peer-reviewed publications: 248 research + 54 reviews + 5 books + 4 edited journals + 5 book reviews. [1]. Hirsh, J. E. (2005), An index to quantify an individual s scientific research output, Proceedings of the National Academy of Sciences of the United States of America, 102 : 16569-16572. [2]. Anderson et al., (2008) Beyond the Durfee square: Enhancing the h-index to score total publication output, Scientometrics, 76; p577-588.

    *Source: Google Scholar.

    Link to Google Scholar Profile

    OUBSU Publications : 2000-2004









    • Schnell, I. and Watts, A. (2001) Towards selective recoupling and mutual decoupling of dipolar-coupled spin pairs in double-quantum magic-angle spinning NMR experiments on multiply labelled solid-state samples, Chemical Physics Letters, 335, 111-122
    • Williamson, P.T.F., Watts, J.A., Addona, G.H. Miller, K.W. and Watts, A. (2001) Dynamics and orientation of N+(CD3)3-bromoacetylcholine bound to its binding site on the nicotinic acetylcholine receptor. PNAS , 98, 2346-2351.
    • Bonev, B.B., Gilbert, R.J.C., Andrew, P.W., Byron, O. and Watts, A. (2001) Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin. J. Biol. Chem., 276, 5714-5719.
    • Bonev, B., Gilbert, R. and Watts, A. (2001) Structural investigations of pneumolysin/lipid complexes. Mol. Memb. Biol., 17, 229-235.
    • Addy, V.L., Covington, A.D., Langridge, D.A. and Watts, A. (2001) Microscopy methods to study fat cells. Part 1: Characterisation of ovine cutaneous lipids using microscopy. J. Soc. Leather Tech. Chem., 85, 6-15.
    • Addy, V.L., Covington, A.D., Langridge, D.A. and Watts, A. (2001) Microscopy Methods to study lipase degreasing. J. Soc. Leather Tech. Chem.
    • Schnell, I., Watts, A. & Spiess, H.W. (2001) Double-quantum double-quantum MAS exchange NMR spectroscopy: dipolar coupled spin-pairs as probes for slow molecular dynamics. J. Mag. Res. 149, 90-102.
    • Bonev, B., Watts, A., Bokvist, M. and Gröbner, G. (2001) Electrostatic peptide-lipid interaction sof amyloid-ß and pentalysine with membrane surfaces monitored by phorphorus-31 MAS NMR. Phys. Chem. Chem. Phys., 3, 2904-2910.
    • Williamson, P.T.F., Bains, S.K., Chung, C., Cooke, R., Meier, B. & Watts, A. (2001) Characterization and assignment of uniformly labeled NT(8-13) at the agonist binding site of the G-protein coupled neurotensin receptor. In: Focus on Structural Biology Vol. 1 Perspectives on Solid State NMR in Biology (Eds. S.R. Kühne & H.J.M. de Groot), Focus on Stuctural Biology, Kluwer Academic Publishers, Dordrecht, pp. 191-202.
    • Gröbner G; Glaubitz C; Williamson PTF; Hadingham T & Watts A. (2001) Structural insights into the insertion of amyloid-beta peptide with biological membranes by solid state NMR. In: Focus on Structural Biology Vol. 1 Perspectives on Solid State NMR in Biology (Eds. S.R. Kühne & H.J.M. de Groot), Kluwer Academic Publishers, Dordrecht, pp. 203-214.
    • Watts, J.A., Watts, A. & Middleton, D.A. (2001) A model of reversible inhibitors in the gastric H+/K+-ATPase binding site determined by REDOR NMR. J. Biol. Chem. 276, 43197-43204.
    • Areas, J.A.G., Cassiano, M.M., Glaubitz, C., Gröbner, G.J. & Watts, A. (2001) Interaction of b-casein at an emulsion interface studied by 2H NMR and molecular modeling. In: Magnetic Resonance in Food Science: A view to the future. Webb, G.A.; Belton, P.S.; Gil, A.M. & Delgadillo, I., Royal Society of Chemistry, Cambridge, UK, pp 193-201.



    OUBSU Publications : 1990-1999

    Scientific papers 1995-9


    Scientific papers 1990-4



    1995 - 1999
    • Ulrich,A.S., Wallat, I., Heyn, M.P. & Watts, A. (1995) Re-orientation of the retinal chromophore in the M-photointermediate of bacteriorhodopsin. Nature Structural Biology, 2, 190-192.
    • Middleton, D.A., Reid, D.G. & Watts, A. (1995) The conformations of a functional spin-labelled derivative of gastric H/K-ATPase investigated by EPR spectroscopy. Biochemistry, 34, 7420-7429.
    • Pinheiro, T.J.T., Elöve, G.A., Roder, H., de Jongh, H.H.J., de Kruijff, B. & Watts, A.(1995) Lipid-mediate folding of apocytochrome c . Proceedings of the Meeting "Perspectives on Protein Engingeering and Complementary Technologies".
    • Venien-Bryan, C., Davies, A., Langmack, K., Baverstock, J., Watts, A., Marsh, D., & Saibil, H. (1995) Effect of the C-terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes. FEBS Lett. 359, 45-49.
    • Watts, A., Sternberg, B., Ulrich, A.S., Whiteway, C.A., Seifert, G., Sami, M., Fisher, P., Heyn, M. & Wallat, I. (1995) Bacteriorhodopsin: the effect of bilayer thickness on 2D array formation, and the structural re-alignment of retinal through the photocycle. Biophysical Chemistry, 56, 41-46.
    • Boulter, J.M., Taylor, A.M. & Watts, A. (1996) Asymmetric and functional reconstitution of band 3 into pre-formed phosphatidylcholine vesicles. Biochim. Biophys. Acta 1280, 265-271
    • Albert, A.D., Boesze-Battaglia, K., Paw, Z., Watts, A., Epand, R.M. (1996) Effect of cholesterol on rhodopsin stability in disk membranes. Biochim. Biophys. Acta. 1297(1): 77-82
    • Biaggi, M.H., Pinheiro, T.J.T., Watts, A., Lamy-Freund, M.T. (1996) Spin label and 2H-NMR studies on the interaction of melanotropic peptides with lipid bilayers. Eur. Biophys. J. ; 24(4): 251-9
    • Cölfen, H., Harding, S.E., Boulter, J.M. & Watts, A. (1996) A hydrodynamic examination of the dimeric cytoplasmic domain of the human erythrocyte anion transporter, band 3. Biophysical J., 71, 1611-1615.
    • Pinheiro, T.J.T., Duer, M.J. & Watts, A. (1997) Phospholipid headgroup dynamics in DOPG-d5-cytochrome c complexes as revealed by 2H and 31P NMR: The effects of a peripheral protein on collective lipid fluctuations. Solid state NMR 8, 55-64.
    • Middleton, D.A., Robins, R., Feng, X., Levitt, M.H., Spiers, I.D., Schwalbe, C., Reid, D.G. & Watts, A. (1997) The conformation of an inhibitor bound to gastric proton pump. FEBS Letts. 410, 269-274.
    • Albert, A.D., Watts, A., Spooner, P.J.R., Grobner, G., Young, J. & Yeagle, P.L. (1997) A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin in rod outer segment disk membranes. Biochim. Biophys. Acta 1328, 74-82.
    • Grobner, G., Choi, G., Burnett, I., Verdegem, P., Lugtenburg, J., Glaubitz, C. & Watts, A. (1997) Photoreceptor rhodopsin: A structural and conformational study of 11-cis retinal in rhodopsin in oriented membranes by deuterium solid state NMR. Biophys. J. 72, A114.
    • Gröbner, G., Taylor, A., Williamson, P.T.F., Choi, G., Glaubitz, C., Watts, J.A., de Grip, W.J. & Watts, A. (1997) Macroscopic orientation of natural and model membranes for structural studies. Analytical Biochemistry, 254,132-136.
    • Pinheiro, T.J.T., Elöve, G.A., Watts, A. & Roder, H. (1997) Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry, 36, 13122-13132
    • Watts, A. and Sabra, M. (1997) Not all integral proteins are freely diffusing in a fluid mosaic: how lipids can promote protein array formation. Biol. Skr. Dan. Vid. Selsk, 49, 123-126.
    • Arêas, J.A.G., Gröbner, G.J., Pellacani, L.B., Glaubitz, C. & Watts, A. (1997) Use of solid state 2H NMR for studying protein-lipid interactions at emulsion interfaces. Mag. Res. in Chemistry 35: S119-S124.
    • Glaubitz, C. and Watts, A. (1998) Magic angle oriented sample spinning (MAOSS): A new approach towards biomembrane studies. J. Mag. Res. 130, 305-316.
    • Addy, V.L., Covington, A.D. and Watts, A. (1998) Enzyme degreasing of animal skins: a biochemical and microscopical study. Proceeding of IULTCS Congress.
    • Grobner, G., Choi, G., Burnett, I., Glaubitz, C. & Watts, A. (1998) Photoreceptor rhodopsin: Structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR. FEBS Lett, 422, 201-204.
    • Duralski, A.A., Spooner, P.J.R., Rankin, S.E. & Watts, A. (1998) Synthesis of isotopically labelled cardiolipins. Tetrahedron Letts., 39, 1607-1610.
    • Arêas, J.A.G., Gröbner, G.J., Glaubitz, C. & Watts, A. (1998) Interaction of a type II myosin with biological membranes studied by 2H solid state NMR. Biochemistry, 37, 5582-5588.
    • Williamson, P.T.F., Gröbner, G., Spooner, P.J.R., Miller, K.W. & Watts, A. (1998) Probing the agonist binding pocket on the nicotinic acetylcholine receptor: a high resolution solid state NMR approach. Biochemistry, 37, 10854-10859.
    • Cölfen, H., Boulter, J., Harding, S.E. and Watts, A. (1998) Ultracentrifugation studies on the transmembrane domain of the human erythrocyte anion transporter Band 3 in the detergent C12E8. Eur. Biophys. J. 27, 651-655.
    • Watts, A., Burnett, I.J., Glaubitz, C., Gröbner, G., Middleton, D.A., Spooner, P.J.R. & Williamson, P.T.F. (1998) Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions. Eur. Biophys. J. 28, 84-90.
    • Rankin, S.E., Watts, A. & Pinheiro, T.J.T. (1998) Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid. Biochemistry, 37, 12588-12595.
    • Sabra, M.C., Uitdehaag, J.C.M. & Watts, A. (1998) General model for lipid-mediated 2D array formation of membrane proteins. Application to bacteriorhodopsin. Biophys. J., 75, 1180-1188
    • Spooner, P.J.R., O'Reilly, W.J., Homans, S.W., Rutherford, N.G., Henderson, P.J.F. & Watts, A. (1998) Weak substrate binding to transport proteins studied by NMR. Biophys. J. 2794-2800.
    • Rankin, S.E., Watts, A., Roder, H. & Pinheiro, T.J.T. (1999) Folding of apolcytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state. Protein Science, 8, 381-393.
    • Taylor, A.M. & Watts, A. (1999) Spin-label studies of lipid-protein interactions with reconstituted Band 3, the human erythrocyte chloride/bicarbonate exchanger. J. Biochem & Cell Biol. 76(5), 815-22.
    • Taylor, A.M., Boulter, J., Harding, S.E. & Watts, A. (1999) Hydrodynamic properties of human erythrocyte Band 3 solubilized in reduced Triton X-100. Biophys. J. 76, 2043-2055.
    • Glaubitz, C., Burnett, I., Gröbner, G., Mason, J. & Watts, A. (1999) Deuterium-MAS NMR spectroscopy on oriented membrane proteins: Application to photointermediates of bacteriorhodopsin. J. Am. Chem. Soc. 121, 5787-5794.
    • Spooner, P.J.R., Veenhoff, L., Watts, A. & Poolman, B. (1999) Structural information on a membrane transport protein from NMR using sequence-selective nitroxide labelling. Biochemistry, 38, 9634-9639.
    • Bryson, E.A., Rankin, S.E., Carey, M., Watts, A. & Pinheiro, T.J.T. (1999) Folding of apocytochrome c in lipid micelles: Formation of a-helix precedes membrane insertion. Biochemistry, 38, 9758 -9767
    • Taylor, A.M., Gröbner, G., Williamson, P.T.F. & Watts, A. (1999) Binding properties of the stilbene disulfonate sites on human erythrocyte AE1: kinetic, thermodynamic and solid state deuterium NMR analyses. Biochemistry, 38, 11172-11179.
    • Gröbner, G, Glaubitz, C and Watts, A. (1999) Probing membrane surfaces and the location of membrane embedded peptides by 13C MAS NMR using lanthanide ions. J. Mag. Res. 141, 335-339.

    1990 - 1994
    • Fraser, D., Louro, S., Horvath, L.I., Miller, K. and Watts, A. (1990) A study of the effect of general anesthetics on lipid-protein interactions in acetylcholine receptor enriched membranes fromTorpedo nobiliana using nitroxide spin-labels. Biochemistry, 29, 2664-2669.
    • Ulrich, A.S., Volke, F. and Watts, A. (1990) The dependence of phospholipid head- group mobility on hydration as studied by deuterium-NMR spin-lattice relaxation time measurements. Chem. Phys. Lipids 55 61-66
    • Ulrich, A.S., Poile, T.W. and Watts, A. (1990) Deuterium NMR to study the surface of phospholipid bilayers. Bull. Mag. Res. 12, 80-83.
    • van Gorkom, L., Horvath, L.I., Hemminga, M.A., Sternberg, B. and Watts, A. (1990) Identification of trapped and boundary lipid binding sites in M13 coat protein-lipid complexes by deuterium NMR spectroscopy. Biochemistry, 29, 3828-3834..
    • Spooner, P.J.R. , Van Gorkom, L.C.M. and Watts, A. (1990) Moderating the heating of biological samples during magic-angle spinning experiments. J. Mag. Res. 90, 584-588.
    • Sanders, J.C., Poile, T.W., Spruijt, R.B., Van Nuland, N.A.J., Watts, A. and Hemminga, M.A. (1991) A NMR investigation on the interactions of the a-oligomeric form of the M13 coat protein with lipids which mimic the Escherichia coli inner membrane. Biochim. Biophys. Acta, 1066, 102-108.
    • Gale, P. & Watts, A. (1991) Characterization of phospholipid compositions and physical properties of DMPC/Bacteriorhodopsin vesicles produced by a detergent-free method. Biochem. Biophys. Res. Comm. 180, 939-944.
    • Fraser, D.M., Van Gorkom, L.C.M. and Watts, A. (1991) Partitioning behaviour of 1- hexanol into lipid membranes as studied by deuterium NMR spectroscopy. Biochim. Biophys. Acta, 1069, 53-60.
    • Spooner, P.J.R. and Watts, A. (1991) Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements. Biochemistry, 30, 3871-3879.
    • Spooner, P.J.R. and Watts, A. (1991) Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements. Biochemistry, 30, 3880-3885.
    • Spooner, P.J.R. and Watts, A. (1992) Cytochrome c interactions with cardiolipin in bilayers: A multinuclear magic-angle spinning NMR study Biochemistry, 31, 10129-10138.
    • Gale, P. & Watts, A. (1992) Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn -glycero-3-phosphocholine in bilayers - a 31P and 2H- NMR study Biochim. Biophys. Acta, 1106, 317-324.
    • Ulrich, A.S., Wallat, I., Heyn, M.P. and Watts, A. (1992) Evidence for a curved retinal in BR from solid-state 2H-NMR. In: Structures and Functions of Retinal Proteins (J.- L. Rigaud, ed.) Colloque INSERM/John Libbey Eurotext Ltd., 221, 247-249.
    • Ulrich, A.S. & Watts, A. (1992) Membrane protein structure determination by deuterium-NMR. Case study: Retinal in bacteriorhodopsin. NATO ASI, 63, 243-249.
    • Fajer, P., Watts, A. and Marsh, D. (1992) Saturation transfer, continuous wave saturation, and saturation recovery electron spin resonance studies of chain-spin labeled phosphatidylcholines in the low temperature phases of dipalmitoyl phosphatidylcholine bilayers: Effects of rotational dynamics and spin-spin interaction. Biophys. J., 61, 879-891.
    • Sami, M., Malik, S. & Watts, A. (1992) Structural stability of the erythrocyte anion transporter, band 3, in native membranes and in detergent micelles. Biochim. Biophys. Acta, 1105, 148-154.
    • Ulrich, A.S., Heyn, M.P. and Watts, A. (1992) Structure determination of the cyclohexene-ring of retinal in bacteriorhodopsin by solid-state deuterium-NMR. Biochemistry, 31, 10390-10399.
    • Sternberg, B., L'Hostis, C., Whiteway, C.A. and Watts, A. (1992) The essential role of Halobacterium halobium lipids in 2D-array formation of bacteriorhodopsin. Biochim. Biophys. Acta, 1108, 21-30.
    • Duralski, A.A. and Watts, A. (1992) Synthesis of isotopically labelled ubiquinones. Tetrahedron Letts, 33, 4983-4984.
    • Areas, J.A.G. and Watts, A. (1993) Interaction of myosin with charged membranes is affected by ATP. Biochemical Society Transactions , 21, 80S.
    • Ulrich, A.S. and Watts, A. (1993) 2H NMR lineshapes of immobilized uniaxially oriented membrane proteins Solid State NMR 2, 21-36.
    • Abadji, V.C., Raines, D.E., Watts, A. and Miller, K.W. (1993) The effect of general anaesthetics on the dynamics of phosphatidylcholine-acetylcholine receptor interactions in reconstituted vesicles. Biochim. Biophys. Acta, 1147, 143-153.
    • Pinheiro, T.J.T., Bratt, P.J., Davis, I.H., Doetschman, D.C. and Watts, A. (1993) Spin- lattice relaxation times of phospholipid aminoxyl spin labels in cardiolipin-cytochrome c bilayers: a pulse saturation-recovery EPR study. J. Chemical Society, Perkin Transactions 2 p.2113-2117
    • Spooner, P.J.R., Duralski, A.A., Rankin, S.E., Pinheiro, T.J.T. and Watts, A. (1993) Dynamics in a protein-lipid complex: NMR measurements of the headgroup of cardiolipin when bound to cytochrome c. Biophysical Journal , 65, 106-112.
    • Heyer-Hartl, M., Brophy, P.J., Marsh, D. and Watts, A. (1993) Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidyglclycerol bilayers, studied by 2H and 31P NMR spectroscopy. Biochemistry32, 9709-9713.
    • Sternberg, B., Watts, A. and Cejka, Z. (1993) Lipid induced modulation of the protein packing in two-dimensional crystals of bacteriorhodopsin. J. Struct. Biology, 110, 196-204.
    • Malik, S., Sami, M. and Watts, A. (1993) A role for Band 4.2 in Human erythrocyte band 3 mediated anion transport. Biochemistry, 32, 10078-10084.
    • Yeagle, P.L., Dentino, A.R., Frazer Smith, T., Spooner, P. and Watts, A. (1993) The anti-viral peptide carbobenzoxy-D-phenylalanine-L-phenylalanine-glycine changes the average conformation of phospholipids in membranes. Biochemistry, 32, 12197- 12202.
    • Ulrich, A.S. and Watts, A. (1994) Lipid headgroup hydration by 2H-NMR: a link between spectroscopy and thermodynamics. Biophysical Chemistry, 49, 39- 50.
    • Renfrey, S. & Watts, A. (1994) Morphological and biochemical characterization of influenza vaccines commercially available in the United Kingdom. Vaccine, 12, 747-751.
    • Pinheiro, T.J.T. and Watts, A. (1994) Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilayers revealed by solid-state 31P NMR. Biochemistry, 33, 2451-2458.
    • Pinheiro, T.J.T. and Watts, A. (1994) Resolution of individual lipids in mixed phospholipid membranes and specific lipid-cytochrome c interactions by magic angle spinning solid-state phosphorus-31 NMR. Biochemistry, 33, 2459-2467.
    • Pinheiro, T.J.T., Duralski, A.J. and Watts, A. (1994) Phospholipid headgroup- headgroup electrostatic interactions in mixed bilayers of cardiolipin with phosphatidylcholines studied by 2H NMR. Biochemistry, 33, 4896-4902.
    • Spooner, P.J.R., Rutherford, N., Watts, A. and Henderson, P.J.F. (1994) NMR observation of substrate in the binding site of an active sugar H+ symport protein in native membranes. PNAS. 91, 3877-3881.
    • Bradshaw, J.P., Dempsey, C.E. and Watts, A. (1994) A combined X-ray and neutron diffraction study of selectively deuterated melittin in phospholipid bilayers: the effect of pH. Mol. Membrane Biol. 11, 79-86.
    • Calder, P.C., Yaqoob, P., Harvey, D.J., Watts, A. and Newsholme, E.A. (1994) Incorporation of fatty acids by concanavalin A-stimulated lymphocytes and the effect on fatty acid composition and membrane fluidity. Biochem. J., 300, 509-518
    • Ulrich, A.S. & Watts, A. (1994) Molecular response of the lipid headgroup to bilayer hydration as monitored by 2H-NMR. Biophysical J., 66, 1441- 1449.
    • Ulrich, A.S., Sami, M. and Watts, A. (1994) Hydration of DOPC bilayers by DSC. Biochim. Biophys. Acta, 1191, 225-230.
    • Ulrich, A.S., Watts, A., Wallat, I. & Heyn, M.P. (1994) Distorted structure of retinal chromophore in bacteriorhodopsin resolved by 2H-NMR. Biochemistry, 33, 5370-5375.


    1990 - 1999
    • Watts, A. (1990) Protein-lipid interactions at membrane surfaces. In: Biophysics of the cell surface (Glazer, R. and Gingell, D. eds) Springer -Verlag, Berlin-Heidelberg. pp 23-50.
    • Watts, A. (1991) Magnetic Resonance Studies of Lipid-Protein Interfaces and Lipophilic Molecule Partitioning In: Molecular and cellular mechanisms of alcohol and anesthetics (E. Rubin, K.W. Miller and S.H. Roth, eds.) Annals of the New York Academy of Science, 625, 653-669.
    • Watts, A. & Spooner, P.J.R. (1991) Phospholipid phase transitions as revealed by NMR. Chem. Phys. Lipids 57, 195-211
    • Watts, A. & Van Gorkom, L.C.M. (1991) Surface organization of lipid bilayers. In: The Structure of Biological Membranes (P. Yeagle ed.) C.R.C. Press Inc., pp.307- 377.
    • Watts, A. (1993) Magnetic resonance studies of phospholipid-protein interactions in bilayers In: Phospholipids Handbook (G. Cevc, ed.) 687-740, Marcel Dekker, New York
    • Watts, A., Venien-Bryan, C., Sami, M., Whiteway, C., Boulter, J. & Sternberg, B. (1993) Lipid-protein interactions in controlled membrane protein array and crystal formation. In: Protein Lipid Interactions, New Comprehensive Biochemistry series (ed. A. Watts), 351- 370, Elsevier, Amsterdam
    • Watts, A. (1994) Magnetic resonance studies of protein-lipid interactions. In: Biological Membranes: Structure, biogenesis and dynamics (ed. J.A.F. Op den Kamp) NATO ASI Series, H82, 79-92.
    • Watts, A. (1994) Non-crystallographic methods to study membrane proteins. In: Biological Membranes: Structure, biogenesis and dynamics (ed. J.A.F. Op den Kamp) NATO ASI Series, H82, 131-138.
    • Watts, A. (1994) High resolution, non-crystallographic structural studies of large integral membrane proteins. Biochemical Society Transactions, 22, 801-805
    • Watts, A. (1994) Red Heat on salted hides. BCL Journal, 37, 130- 133.
    • Watts, A. (1994) Bacteriorhodopsin: The mechanism of 2D-array formation and the structure of the retinal in the protein. Biophysical Chemistry, 55, 137-151.
    • Watts, A., Ulrich, A.S. & Middleton, D.A. (1995) Membrane protein structure: the contribution and potential of novel solid state NMR approaches. Mol. Membrane Biol., 12, 233-246
    • Watts, A. (1995) Biophysics of the membrane interface. Biochemical Society Transactions, 23, 959-965.
    • Watts, A. (1997) Structural and functional consequence of long-chain polyunsaturation in biomembranes. Prenat. Neonat. Med. 2, 1-11.
    • Watts, A. & Pinheiro, T.J.T. (1998) Biophysics of the membrane interface. In: Membrane protein insertion and translocation. (ed. D. Phoenix), 1-17, Pub. Portland Press.
    • Watts, A. (1998) Solid state NMR approaches for studying the interaction of peptides and proteins with membranes. Biochem. Biophys. Acta, 1376, 297-318.
    • Watts, A. (1999) NMR of drugs and ligands bound to membrane receptors. Current Opinion in Biotechnology, 10, 48-53.
    • Watts, A. (1999) Structural resolution of ligand-receptor interactions in functional, membrane-embedded receptors and proteins using novel, non-perturbing solid state NMR methods. Pharmacy & Pharmacology Communications, 5, 7-13.
    • Watts, A. & Middleton, D. (1999) Biological solid state NMR comes of age: NMR to study non-crystalline, heterogeneous biological complexes with no size of molecular weight limit. The Biochemist, 19, 11-17.
    • Watts, A., Burnett, I.J., Glaubitz, C.,Gröbner, G., Middleton, D.A., Spooner, P.J.R., Watts, J.A. & Williamson, P.T.F. (1999) Membrane protein structure determination by solid state NMR. Natural Product Reports, 16, 419-423.

    OUBSU Publications : pre-1990

    Scientific papers

    1972 - 1979


    1980 - 1989



    1972 - 1979
    • Marsh, D., Phillips, A.D., Watts, A. and Knowles, P.F. (1972) A spin-label study of Fractionated Egg Phosphatidyl Choline Vesicles. Bioch. Biophys. Res. Comm. 49, 641-648.
    • Marsh, D., Watts, A. and Knowles, P.F. (1977) Cooperativity of the Phase Transition in Single- and Multibilayer Lipid Vesicles. Biochim. Biophys. Acta 465, 500- 514.
    • Marsh, D., Watts, A. and Knowles, P.F. (1976) Evidence for Phase Boundary Lipid. Permeability of Tempocholine into Dimyrostoyl-Phosphatidylcholine Vesicles at the Phase Transition, Biochemistry 15, 3570-3578.
    • Watts, A., Marsh, D. and Knowles, P.F. (1978) Lipid-substituted cytochrome oxidase: no absolute requirement of cardiolipin for activity Bioch. Biophys. Res. Comm. 81, 403-409.
    • Watts, A., Harlos, K., Maschke, W. and Marsh, D. (1978) Control of Structure and Fluidity of Phosphatidylglycerol Bilayers by pH-Titration. Biochim. Biophys. Acta 510, 63-74.
    • Marsh, D. and Watts, A. (1978) NMR spin-spin splittings in Lipid Membranes. Headgroup conformation in phosphatidylglycerol bilayers. FEBS Letts. 85, 124-126.
    • Marsh, D., Watts, A., Maschke, W. and Knowles, P.F. (1978) Protein-immobilized Lipid in DMPCûsubstituted cytochrome oxidase: Evidence for both Boundary and trapped-Bilayer Lipid. Bioch. Biophys. Res. Comm. 81, 397-402.
    • Watts, A., Marsh, D. and Knowles, P.F. (1978) Characterisation of DMPC vesicles and their dimensional changes through the phase transition - Molecular control of membrane morphology. Biochemistry 17, 1792-1801.
    • Knowles, P.F., Watts, A. and Marsh, D. (1979) Spin-label studies of lipid immobilization in DMPC-substituted cytochrome oxidase. Biochemistry 18, 4480-4487.
    • Dowdall, M.J., Fohlman, J.P. and Watts, A. (1979) Presynaptic Action of Snake Venom Neurotoxins in Cholergic Systems. Adv. in Cytopharmacology 3, 63-76.
    • Watts, A., Volotovski, I.D. and Marsh, D. (1979) Rhodopsin-Lipid Associations in Bovine Rod Outer Segment Membrane. Identification of Immobilized lipid by Spin-labels. Biochemistry 18, 5006-5013.

    1980 - 1989
    • Watts, A. and Marsh, D. (1980) Fusion of dipalmitoylphosphatidylcholine vesicles. Fed. Proc. 39, 1984.
    • Fretten, P., Morris, S.J., Watts, A. and Marsh, D. (1980) Lipid-lipid and Lipid-protein Interactions in Chromaffin Granule Membranes. A spin-label ESR study. Biochim. Biophys. Acta 598, 247-259.
    • Marsh, D. and Watts, A. (1980) Molecular Motion in Phospolipid Bilayers in the Gel Phase: Spin-label Saturation Transfer ESR Studies. Bioch. Biophys. Res. Comm. 94, 130-137.
    • Cevc, G., Watts, A. and Marsh, D. (1980) Non-electrostatic contribution to the Titration of the Ordered-fluid phase Transition of Phosphatidylglycerol Bilayers. FEBS Letts. 120, 267-270.
    • Watts, A. (1980) Novel Applications of the Analytical Ultracentrifuge: Molecular Weight and Morphological Studies on Phospholipid vesicles. Biochem. Soc. Trans. 8, 522-523.
    • Watts, A., Davoust, J., Marsh, D. and Devaux, P.F. (1981) Distinct States of lipid mobility in bovine rod outer segment membranes. Biochim. Biophys. Acta 643, 673-676.
    • Watts, A. Harlos, K. and Marsh, D. (1981) Charge-induced Tilt in ordered-phase phosphatidylglycerol bilayers. Evidence from X-ray diffraction. Biochim. Biophys. Acta 645, 91-96.
    • Knowles, P.F., Watts, A. and Marsh, D. (1981) Spin-label studies of head-group specificity in the interaction of phospholipids with yeast cytochrome oxidase Biochemistry 20, 5888-5894.
    • Marsh, D., Watts, A. and Barrantes, F.J. (1981) Phospholipid Chain Immobilization and Steroid Rotational Immobilization in Acetylcholine Receptor-rich Membranes for Torpedo marmorata. Biochim. Biophys. Acta 645, 97-101.
    • Watts, A. and Marsh, D. (1981) Saturation Transfer ESR studies of molecular motion in phosphatidylglycerol bilayers in the gel phase. Effects of pre-transitions and pH titration. Biochim. Biophys. Acta , 642, 231-241.
    • Watts, A., Volotovski, I.D. and Marsh, D. (1981) The motional properties of rhodopsin and the membrane lipids in bovine rod outer segment disc membranes. Biochem. Soc. Trans. 9, 150-151.
    • Cevc, G., Watts, A. and Marsh, D. (1981) Titration of the phase transition of phosphatidyl serine bilayer membranes. Biochemistry 20, 4955-4965.
    • Marsh, D., Watts, A., Knowles, P.F., Pates, R.D., Uhl, R. and Esmann, M. (1982) ESR spin-label studies of lipid protein interactions in membranes. Biophys. J. 37, 265-274.
    • Sixl, F. and Watts, A. (1982) Interactions between phospholipid head groups at membrane interfaces: A deuterium and phosphorous magnetic resonance and spin-label electron spin resonance study. Biochemistry 24, 6446-6452.
    • Watts, A., Volotovski, I.D., Pates, R.D. and Marsh, D. (1982) Spin-label studies of rhodopsin-lipid interactions. Biophysics J. 37, 94-95.
    • Harris, J., Power, T.J., Bieber, A.L. and Watts, A. (1983) An electronspin resonance spin-label study of the interaction of purified Mojave toxin with synaptosomal membranes from rat brain. Eur. J. Biochemistry 131, 559-565.
    • Marsh, D., Watts, A. and Smith, I.C.P. (1983) Dynamic structure and phase behaviour of dimyristoyl phosphatidylethanolamine bilayers studied by deuterium nuclear magnetic resonance. Biochemistry 22, 3023-3026.
    • Sixl, F. and Watts, A. (1983) Headgroup interactions in mixed phospholipid bilayers.Proc. Natl. Acad. Sci. U.S.A. 80, 1613-1615.
    • Sixl, F. , Brophy, P.J. and Watts, A. (1984) Selective protein-lipid interactions at membranes surfaces: a deuterium and phosphorus NMR study of the association of myelin basic protein with the bilayer head groups of DMPC and DMPG Biochemistry 23,2032-2039.
    • Leuschner, J.T.A., Wing, D.R., Harvey, D.J., Brent, G.A., Dempsey, C.E., Watts, A. and Paton, W.D.M. (1984) The partitioning of Tetrahydrocannabinol into erythrocyte membranes in vivo and its effects on membrane fluidity. Experientia 40, 866-868.
    • Tse, A.G.D., Barclay, A.N., Watts, A. and Williams, A.F. (1985) A glycophospholipid tail at the carboxyl terminus of Thy-1 glycoprotein of neurons and thymocytes. Science230, 1003-1008.
    • Alecio, M.R., Miller, A. and Watts, A. (1985) Diffraction of X-rays by rippled phosphatidylcholine bilayers. Biochim. Biophys. Acta 815, 139-142.
    • Volotovski, I.D., Ryba, N.J.P. and Watts, A. (1985) Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles. Biochem. Biophys. Res. Comm. 129, 517-521.
    • Pates, R.D., Watts, A., Uhl, R. and Marsh, D. (1985) Lipid-protein interactions in frog rod outer segment disc membranes. Characterisation by spin-labels. Biochim. Biophys. Acta 814, 389-397.
    • Esmann, M., Watts, A. and Marsh, D. (1985) Spin-label studies of lipid-protein interactions in (Na+, K+)-ATPase membranes from rectal glands of Squalus acanthias. Biochemistry 24, 1386-1393.
    • Sixl, F. and Watts, A. (1985) Deuterium and phosphorus NMR studies on the binding of polymyxin-B to lipid bilayers-water interfaces. Biochemistry 24, 7906- 7910.
    • Ryba, N.J.P., Dempsey, C.E. and Watts, A. (1986) Protein-lipid interactions at membrane surfaces: A deuterium and phosphorus NMR study of the interaction between bovine rhodopsin and the bilayer head-groups of DMPC. Biochemistry, 25, 4818- 4825.
    • Volotovski, I.D., Ryba, N.J.P. and Watts, A. (1986) Calmodulin binding to bovine rod outer segment disc membranes. Doklady 30, 372-375.
    • Watts, A. and Poile, T.W. (1986) Direct determination by 2H NMR of the ionization state of phospholipids and of a local anaesthetic at the membrane surface. Biochim. Biophys. Acta , 861, 368-372.
    • Dempsey, C.E., Ryba, N.J.P. and Watts, A. (1986) Evidence from deuterium Nuclear Magnetic Resonance for the Temperature-dependent reversible Self-association of Erythrocyte Band 3 in Dimyristoyl Phosphatidylcholine Bilayers. Biochemistry 25, 2180- 2187.
    • Datema, K.P., Wolfs, J.A.M., Marsh, D., Watts, A. and Hemminga, M.A. (1987) Spin- label ESR study of bacteriophage M13 coat protein incorporation into mixed lipid bilayers Biochemistry 26, 7571-7574.
    • Dempsey, C.E. and Watts, A. (1987) A deuterium and phosphorus-31 nuclear magnetic resonance study of the interaction of melittin with DMPC bilayers and the effect of contaminating phospholipase A2. Biochemistry 26, 5803-5811.
    • Sizer, P.J.H., Miller, A. and Watts, A. (1987) Functional reconstitution of the integral membrane proteins of influenza virus into phospholipid liposomes. Biochemistry 26, 5106-5113.
    • Dempsey, C.E., Cryer, G. and Watts, A. (1987) Interaction of amino-deuteromethylated melittin with phospholipid membranes as studied by D-NMR. FEBS Lett. 218, 173-177.
    • Ryba, N.J.P., Horvßth, L.I., Watts, A. and Marsh, D. (1987) Molecular exchange at the lipid rhodopsin interface: Spin-label ESR studies of rhodopsin - DMPC recombinants. Biochemistry 26, 3234-3240.
    • Rowntree, J. I. and Watts, A. (1988) Electron spin resonance study of light induced conformational changes in nitroxide labelled bovine rhodopsin. Biochem. Biophys. Res. Comm. 155, p1412-1417.
    • Bradshaw, J.P., Edenborough, M.S., Sizer, P.J.H. and Watts, A. (1989) A description of the phospholipid arrangement intermediate to the humidity produced La and HII phases in dioleoylphosphatidylcholine and its modification by dioleoylphosphatidylethanolûamine as studied by X-ray diffraction. Biochim. Biophys. Acta 987 104-110.
    • Boggs, J.M., Rangaraj, G. and Watts, A. (1989) Behaviour of spin-labels in a variety of interdigitated lipid bilayers. Biochim. Biophys. Acta , 981, p243-253.
    • Dempsey, C. E., Bitbol, M. and Watts, A. (1989) Interaction of melittin with mixed phospholipid membrane bilayers of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR. Biochemistry, 28, 6590-6596.
    • Bradshaw, J.P., Edenborough, M.S., Sizer, P.J.H. and Watts, A. (1989) Observation of rippled dioleoylphosphatidylcholine bilayers by neutron diffraction. Biochim. Biophys. Acta 987 111-114.
    • Wolfs, C. J.A.M., Horvath, L.I., Marsh, D., Watts, A. and Hemminga, M. (1989) Spin- label ESR of bacteriophage M13 coat protein in mixed lipid bilayers, Biochemistry 28, p9995-10001.
    • Duralski, A.A., Spooner, P.J.R. and Watts, A. (1989) Synthesis of optically active polyunsaturated diacylglycerols, Tetrahedron, 30, p3585-3588.
    • Sternberg, B., Gale, P. and Watts, A. (1989) The effect of temperature and protein content on the dispersive properties of bacteriorhodopsin from H. halobium in reconstituted DMPC complexes free of endogenous purple membrane lipids: A freeze fracture electron microscopic study. Biochim.. Biophys. Acta 980, p117-126.
    • Bitbol, M., Dempsey, C.E., Watts, A. and Devaux, P.F. (1989) Weak interaction of spectrin with phosphatidylcholine-phosphatidylserine multilayers: a 2H and 31P NMR study. FEBS Letts. 244, p217-222.


    1980 - 1989
    • Watts, A. (1981) Protein-lipid Interactions. Nature 294, 512.
    • Marsh, D. and Watts, A. (1981) ESR spin-label studies of liposomes. In: Liposomes: From Physical Structure to Therapeutic Applications. (ed. C.G. Knight), Elsevier, Amsterdam, pp. 139-186.
    • Marsh, D. and Watts, A. (1982) Diffusable spin-labels used to study lipid-protein interactions with rhodopsin and bacteriorhodopsin, In: Methods in Enzymology (eds. Colowick and Kaplan) vol. 88, Academic Press, N.Y.
    • Watts, A. (1982) Magnetic Resonance Studies of vertebrate rod outer segments, Ch. 5 In: Progress in Retinal Research, Vol. 1, (eds. Osborne, N.N. and Chader, J.G.) Pergamon Press, Oxford.
    • Marsh, D. and Watts, A. (1982) Spin-labelling and lipid-protein interactions in membranes. Ch. 2 In: Lipid-protein Interactions (Eds. P.C. Jost and O. Hayes Griffith) Vol. 2, Wiley-Interscience, New York - Brisbane - Chichester - Toronto.
    • Watts, A., Sixl, F., Ryba, N.J.P., Dempsey, C.E. and Brophy, P.J. (1985) Deuterium and phosphorus NMR studies of lipid-lipid and lipid-protein interactions in membranes, In: Magnetic Resonance in Biology and Medicine, pp. 349-361 (Govil, Khetrapal, & Saran eds).
    • Watts, A. (1985) Deuterium Nuclear Magnetic Resonance Studies of membrane surfaces, In: Proc. of III Intl. congress on structure and function of biological membranes. Varna, Bulgaria.
    • Watts, A. (1985) Spin-labels in Biochemistry. Biochem. Soc. Trans. 13, 588-593.
    • Watts, A. (1985) Spin-labels to study protein-lipid interactions in membranes, In: Proc. of III Intl. Congress on structure and function of biological membranes, Varna, Bulgaria.
    • Watts, A. (1985) Deuterium and phosphorus NMR studies of membrane surfaces. Studia Biophysica 110, 149-154.
    • Watts, A. (1985) Magnetic resonance studies of vertebrate rod outer segments. Biochem. Soc. Trans. 11, 674-676.
    • Watts, A. (1987) Deuterium and phosphorus NMR studies of membrane surfaces.Bulletin of Mag. Resonance 9, 66-70.
    • Watts, A. (1987) Molecular Dynamics and selectivity in biomembranes, In: Membrane Receptors, Dynamics,and Energetics (Wirtz, K.A.W. ed.) Plenum Press, NATO ASI Series.
    • Watts, A. (1987) NMR methods to characterize lipidûprotein interactions at membrane surfaces, In: J. of Bioenergetics and Biomembranes 19, 625-653 (Sanadi, D.R. ed.), Plenum Pub. Co, 625-653.
    • Watts, A. (1988) Magnetic resonance studies of molecular dynamics at membrane surfaces. In: Dynamic properties of biomolecular assemblies (Harding, S. and Rowe, A.J. eds) Royal Chemical Society, 320-347.
    • Marsh, D. and Watts. A. (1988) Association of lipids with membrane proteins, in: Recent Advances n Membrane Fluidity, vol. 4 (Aloia, R. ed.) Alan R. Liss, Inc., New York, 2, 163-200.
    • Watts, A. (1988) Probing membrane surfaces by NMR. Studia Biophysica. 127, p29-36.
    • Watts, A. (1989) Membrane structure and dynamics. Current opinions in cell biology, Vol. 4, (Warren, G.B. & Simons, K. eds) Current Science, London.

    Theses and Reports


    Year Author Title
    2014 Steven Lavington



    2015 Alice Hart

    The Role of β-Arrestin Finger Loop

    Residues in GPCR Binding Affinity

    2015 Patricia Dijkman

    Biophysical Studies of Membrane Protein Structure and Function

    2014 Roslin Adamson Probing GPCR-Gα interactions : a functional study by EM and SPR
    2012 Olivia Berthoumieu

    Single Molecule Studies of Seven Transmembrane Domain Proteins

    2011 Marcella Orwick Biophysical and Magnetic Resonance Studies of Membrane Proteins
    2009 Satita Tapaneeyakorn Towards NMR spectrocopic studies of the NTS1-NT complex
    2008 Peter Judge Kinetics and modulation of the viral ion channel VPU from HIV-1
    2007 Lubica Aslimovska High resolution structural studies of membrane proteins using solid state NMR
    2007 Peter Harding A biophysical study of the G-protein coupled receptor neurotensin receptor 1
    2006 Timothy Hadingham Biophysical studies of the G-protein coupled neurotensin receptor
    2005 Chang Gyeom Kim Probing structures of membrane proteins and their inhibitors
    2004 Vincent Lemaitre Non-covalent interactions in biomolecules studied by 17O NMR and MD simulations
    2003 Jonathan Sharples The conformation of the β-ionone ring region of the chromophore of rhodopsin, in the dark and meta-I photostates
    2002 Scott Goodall Probing the structure of acetylcholinesterase inhibitors in their binding site using solid state nuclear magnetic resonance
    2001 James Mason Solid-state NMR Studies of bacteriorhodopsin and the purple membrane
    2001 Jude Watts Probing inhibitor binding sites of the gastric H/K-ATPase
    2000 Zareen Ahmed Magnetic resonance spectroscopy of phospholamban and its interaction with Ca2+-ATPase
    1999 Phil Williamson The application of solid state nuclear magnetic resonance to the study of ligand protein interactions
    1998 Clemens Glaubitz Probing structures of membrane proteins and their inhibitors

    Post-doctoral vacancies

    Currently there are no advertised vacancies for post-doctoral researchers in the Biomembrane Structure Unit.

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    There are no current funded vacancies for post-graduate students.

    Enquiries are always welcomed from researchers with appropriate qualifications who would like to expand either their NMR experience into the biological field or their biochemistry/chemistry experience into the solid state NMR field to resolve the structure and dynamics of membrane proteins.

    Informal enquiries should be addressed to Professor A. Watts by email

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