Bonnie Ann Wallace

Professor of Molecular Biophysics
Institute of Structural and Molecular Biology
Birkbeck College
University of London
London WC1E 7HX U.K.

phone: 44-(0)207-631-6800
fax: 44-(0)207-631-6803
email: b.wallace@mail.cryst.bbk.ac.uk

Ph.D.(Molecular Biophysics and Biochemistry), Yale University
Jane Coffin Childs Postdoctoral Fellow, Harvard University
Jane Coffin Childs Postdoctoral Fellow, MRC Lab of Molecular Biology, Cambridge

Fellow, AAAS
Fellow, Institute of Biology
Fellow, Royal Society of Chemistry
Fellow, International Union of Pure and Applied Chemistry
Honorary Member, British Biophysical Society

Fellow, (US) Biophysical Society

Royal Society of Chemistry Interdisciplinary Prize
AstraZeneca Award from the Biochemical Society
Dayhoff Award of the Biophysical Society

Camile and Henry Dreyfus Teacher-Scholar Award
Irma T. Hirschl Award

Book on CD and SRCD:
"Modern Techniques for Circular Dichroism and Synchrotron Radiation Circular Dichroism Spectroscopy"

B.A. Wallace and R.W. Janes, Editors
click here for information on contents and how to order

The main focus of my lab is on structure/function studies of membrane proteins, especially those involved in ion translocation and transport. Of particular interest are voltage-gated sodium channels: we have determined the first crystal structure of a sodium channel in its open conformation . We have also determined the first crystal structures of complexes of a sodium channel with several eukaryotic sodium channel drugs, which we have shown block prokaryotic channels, making this channel an excellent candidate for drug discovery/development, and we identified for the first time the locations of the sodium ions in the channel, and determined the structure of a full-length open activated sodium channel which has revealed a novel interaction motif and has identified residues conserved across human and prokaryotic channels, that are associated with disease states. To do these studies, my lab uses the techniques of X-ray crystallography, cryoEM, circular dichroism spectroscopy, biophysical characterisation methods, cloning and expression, bioinformatics, and molecular modelling. We also correlate structure/function studies by molecular dynamics calculations and use a range of functional studies (many in collaborative studies with electrophysiology experts (including the Clapham, DeCaen, and Hemmings labs) to examine structure/function relationships for ion channels. We have determined the conformational changes associated with channel opening and closing, and the locations of a number of widely used drugs within the channel hydrophobic core and in the intramembranous fenstrations, whilst showing the effects of mutations on drug binding. These studies extend our early crystalllography and NMR structure/function studies on polypeptide ion channels, including peptaibols, gramicidin and alamethicin, which led to the first detailed molecular views of ion channels.

The other main focus of my lab is the development of techniques and applications for circular dichroism spectroscopy, including the method of synchrotron radiation circular dichroism (SRCD) spectroscopy of proteins, and the application of circular dichroism spectroscopy for the study of  membrane proteins, including ways of mitigating solvent shifts, differential scattering, and absorption flattening effects in such samples. We have created the widely-used (>1 million analyses)  DICHROWEB website for secondary structural calculations, which also includes our new soluble and membrane protein reference databases for CD analyses, and a  CD data processing, analysis and archive package "CDtoolX" for use with conventional CD and SRCD data. In a collaborative project with R.W. Janes of Queen Mary, University of London, we have created the the only deposition and archiving data bank for circular dichroism spectra, the Protein Circular Dichroism Data Bank (PCDDB), (and its associated with validation software, Validichro, and the DichroMatch method for structural analyses).  These tools have all found major use for the analyses of circular dichroism data by groups worldwide.

Selected Publications:

  • Chen, Y., Tucker, A., and Wallace, B.A. (1996) Solution Structure of a Parallel Left-handed Double Helical Gramicidin-A Determined by 2D 1H NMR. J. Mol. Biology 264:757-769.
  • Doyle, D. and Wallace, B.A. (1997) The Crystal Structure of a Gramicidin/ Potassium Thiocyanate Complex. J. Mol. Biology 266:963-977.
  • Wallace, B.A. and Corder, R. (1997) Circular Dichroism Studies of Human Big-Endothelin (BigET). J. Peptide Research 49:331-335.
  • Chen, Y. and Wallace, B.A. (1997) Solvent Effects on the Conformation and Far UV CD Spectra of Gramicidin. Biopolymers 42:771-781.
  • Riley, M.L., Wallace, B.A., Flitsch, S.L., and Booth, P.J. (1997) Slow alpha helix formation during folding of a membrane protein. Biochemistry 36:192-196.
  • Chen, Y. and Wallace, B.A. (1997) Secondary Solvent Effects on the Circular Dichroism Spectra of Polypeptides: Influence of Polarisation Effects on the Far Ultraviolet Spectra of Alamethicin. Biophysical Chemistry 65:65-74.
  • Doyle, D.A. and Wallace, B.A. (1998) Directing the Equilibrium Mixture of Gramicidin Double Helices Towards a Single Conformation with Multivalent Cationic Salts. Biophysical J. 75:635-640.
  • Wallace, B.A. (1998) Recent Advances in the High Resolution Structures of Bacterial Channels: Gramicidin A. J. Structural Biology 121:123-141.
  • Snook, C., Oliva, G., Pattabhi, V., Wood, S., Blundell, T., and Wallace, B.A. (1998) The Structure of Antiamoebin, a Proline-Rich Membrane-Active Polypeptide. Structure 6:783-792.
  • Duclohier, H., Snook, C.F. and Wallace, B.A. (1998) Antiamoebin Can Function as a Carrier or as a Pore-Forming Peptaibol. BBA (Biomembranes) 1415:255-260.
  • Rodi, D.J., Janes, R.W., Sanganee, H.J., Holton, R.A., Wallace, B.A., and Makowski, L. (1999) Screening of a Library of Phage-displayed Peptides Identifies Human Bcl-2 as a Taxol-binding Protein. J. Mol. Biology 285:197-203./
  • Cronin, N. and Wallace, B.A. (1999) Do the Structures of Big ET-1 and Big ET-3 Adopt a Similar Overall Fold? Consequences for Endothelin Converting Enzyme Specificity. Biochemistry 38:1721-1726.
  • Hanlon, M.R., Berrow, N.S., Dolphin, A.C., and Wallace, B.A. (1999) Modelling of the Voltage-Dependent Ca++ Channel Beta subunit as a Basis for Understanding its Functional Properties. FEBS Letts. 445:366-370.
  • Wallace, B.A. (1999) Circular Dichroism Spectrsocopy and X-ray Crystallography: A Dynamic Duo. CCP4 Newletter 37:29-30.
  • Wallace, B.A. and Janes, R.W. (1999) Tryptophans in Membrane Proteins: X-ray Crystallographic Analyses. Adv. Exp. Med. Biol. 467:789-799.
  • Snook, C.P. and Wallace, B.A. (1999) The Molecular Replacement Solution of an Intermediate-Sized Polypeptide, Antiamoebin I. Acta Cryst. D55:1539-1545.
  • Wallace, B.A. (2000) Common Structural Features in Gramicidin and Other Ion Channels. Bioessays 22:227-234.
  • Wallace, B.A. (2000) Conformational Changes by Synchrotron Radiation Circular Dichroism Spectroscopy. Nature Structural Biology 7:708-709.
  • Fischer, W.B., Pitkeathly, M., Wallace, B.A., Forrest, L.R., Smith, G.R., and Sansom, M.S.P. Transmembrane Peptide NB of Influenza B: A Simulation, Structure, and Conductance Study. Biochemistry 39:12708-12716.
  • Hanlon, M.R., Begum, R.R. Newbold, R.J., Whitford, D., and Wallace, B.A. In vitro membrane-inserted conformation of the cytochrome b5 tail. Biochemical Journal 352:117-124.
  • Cid, G.M., Nugent, P.G., Davenport, A.P., Kuc, R.E., and Wallace, B.A. (2000) Expression and Characterisation of the Human Endothelin A Receptor in Pichia pastoris: Influence of N-terminal Epitope Tags. J. Cardio. Pharm. 36:S55-S56.
  • Wallace, B.A. (2000) Synchrotron Radiation Circular-Dichroism Spectroscopy as a Tool for Investigating Protein Structures. J. Synchrotron Radiation 7:289-295.
  • Clarke, DT., Bowler, M.A., Fell, B.D., Flaherty, J.V., Grant, A.F., Jones, G.R., Martin-Fernandez, M.L., Shaw, D.A., Todd, B., Wallace, B.A., and Towns-Andrews, E. (2000) A high aperature beamline for vacuum ultraviolet circular dichroism on the SRS. Synchrotron Radiation News 13:21-27.
  • Orry, A.J.W. and Wallace, B.A. (2000) Modeling and Docking the Endothelin G-Protein Coupled Receptor. Biophysical J. 79:3083-3094.
  • Orry, A.J.W., Janes, R.W., Sarra, R., Hanlon. M.R., Wallace, B.A. (2001) Synchrotron Radiation Circular Dichroism Spectroscopy: Vacuum Ultraviolet Irradiation Does Not Damage Protein Integrity. J. Synchrotron Radiation 8:1027-1029.
  • Chugh, J.K. and Wallace, B.A. (2001) Peptaibols: Models for Ion Channels. Biochemical Society Transactions 29:567-571.
  • Wallace B.A. and Janes, R.W. (2001) Synchrotron Radiation Circular Dichroism Spectroscopy of Proteins: Secondary Structure, Fold Recognition and Structural Genomics. Curr. Opin. Chemical Biology 5:567-571.
  • Hanlon, M. and Wallace, B.A. (2002) Structure and Function of Voltage Dependent Ion Channel Regulatory Beta Subunits. Biochemistry 41:2886-2894.
  • Lobley, A., Whitmore, L., and Wallace, B.A. (2002) DICHROWEB: An Interactive Website for the Analysis of Protein Secondary Structure from Circular Dichroism Spectra. Bioinformatics 18:211-212.
  • Wallace, B.A. (2002) First International Workshop on SRCD Spectroscopy. Synchrotron Radiation News 15:20-22.
  • Lawton, D.G., Longstaff, C., Wallace, B.A., Hill, J., Leary, S.E.C., Titball, R.W., and Brown, K.A. (2002) Interactions of the Type III Secretion Pathway Proteins LcrV and LcrG from Yersinia pestis are Mediated by Coiled-Coil Domains. J. Biol. Chem. 277: 38714-38722.
  • Porcelli, I., de Leeuw, E., Wallis, R., van den Brink-van der Lann, E., de Kruijff, B., Wallace, B.A., Palmer, T., and Berks, B.C. (2002) Characterization and Membrane Assembly of the TatA Component of the Escherichia coli Twin-Arginine Protein Transport System. Biochemistry 41:13690-13697.
  • Chugh, J.K., Bruckner, H., and Wallace, B.A. (2002) Model for a Helical Bundle Channel Based on the High-Resolution Crystal Structure of Trichotoxin_A50E. Biochemistry 41:12934-12941. [journal cover]
  • Lees, J.G., and Wallace, B.A. (2002) Synchrotron Radiation Circular Dichroism and Conventional Circular Dichroism Spectroscopy: A Comparison. Spectroscopy 16:121-125.
  • O'Boyle, F., and Wallace, B.A. (2003) The Temperature Dependence of Gramicidin Conformational States in Octanol. Protein Peptide Letters 10:9-17.
  • Galbraith, T.P., Harris, R., Driscoll, P.C., Wallace, B.A. (2003) Solution NMR Studies of Antiamoebin, a Membrane Channel-Forming Polypeptide. Biophysical J. 84:185-194.
  • Cronin, N.B., O'Reilly, A.O., Duclohier, H., Wallace, B.A. (2003) Binding of the Anticonvulsant Drug Lamotrigine and the Neurotoxin Batrachotoxin to Valtage-gated Sodium Channels Induces Conformational Changes Associated with Block and Steady-state Activation. J. Biol. Chem. 278:10675-10682.
  • Wallace, B.A., Lees, J.G., Orry, A.J.W., Lobley, A., and Janes, R.W. (2003) Analyses of Circular Dichroism Spectra of Membrane Proteins. Protein Science 12:875-884.
  • Wallace, B.A. and Janes, R.W. (2003) Circular Dichroism and Synchrotron Radiation Circular Dichroism Spectroscopy: Tools for Drug Discovery. Biochemical Transactions 31:631-633.
  • O'Reilly, A.O. and Wallace, B.A. The Peptaibol Antiamoebin as a Model Ion Channel: Similarities to Bacterial Potassium Channels. J. Pept. Sci. 9:769-775.
  • Whitmore, L., Chugh, J.K., Snook, C.F. and Wallace, B.A. The Peptaibol Database - A Sequence and Structure Resource. J. Pept. Sci. 9:663-665.
  • Miles, A.J., Wien, F., Lees, J.G., Rodger, A., Janes, R.W., and Wallace, B.A. (2003) Calibration and Standardisation of Synchrotron Radiation Circular Dichroism (SRCD) Amplitudes and Conventional Circular Dichroism (CD) Spectrophotometers. Spectroscopy 17:653-661.
  • Wallace, B.A., Wien, F., Miles, A.J., Lees, J.G., Hoffman, S.V., Evans, P., Wistow, G.J., and Slingsby, C. (2004) Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs. Faraday Discussions 17:653-661.
  • Whitmore, L. and Wallace, B.A. (2004) DICHROWEB, An Online Server For Protein Secondary Structure Analyses from Circular Dichroism Spectroscopic Data. Nucleic Acids Research 32:W668-673.
  • Duclohier, H., Alder, G.M., Bashford, C.L., Bruckner, H., Chugh, J.K., and Wallace, B.A. 2004. Conductance Studies on Trichotoxin_A50E and Implications for Channel Structure. Biophysical J. 87:1705-1710.
  • Whitmore, L., and Wallace, B.A. (2004) The Peptaibol Database: A database for sequences and structures of naturally occurring peptaibols. Nucleic Acids Research 32: D593-D594.
  • Evans, P., Wyatt, K., Wistow, G.J., Bateman, O.A., Wallace, B.A., and Slingsby, C. (2004) The P23T Cataract Mutation Causes Loss of Solubility of Folded gD-Crystallin. J. Mol. Biology 343:435-444.
  • Lees, J.G., Smith, B.R., Wien, F., Miles, A.J., and Wallace, B.A.. (2004) CDtool - An Integrated Software Package for Circular Dichroism Spectroscopic Data Processing, Analysis and Archiving. Analytical Biochemistry 332:285-289.
  • Miles, A.J., Whitmore, L., and Wallace, B.A. (2005) Spectral Magnitude Effects on the Analyses of Secondary Structure from Circular Dichroism Spectroscopic Data. Protein Science 14:368-374.
  • Miles, A.J., Wien, F., and Wallace, B.A. (2004) Redetermination of the Extinction Coefficient of Camphor-b-Sulfonic Acid, a Calibration Standard for Circular Dichroism Spectroscopy. Analytical Biochemistry 335:338-339.
  • Miles, A.J., Wien, F., Lees, J.G., and Wallace, B.A. (2005) Calibration and Standardisation of Synchrotron Radiation and Conventional Circular Dichroism Spectrometers. Part 2: Factors Affecting Magnitude and Wavelength. Spectroscopy 19:43-51.
  • Cronin, N.B., O'Reilly, A., Duclohier, H., and Wallace, B.A. (2005) Effects of Deglycosylation of Sodium Channels on their Structure and Function. Biochemistry 44:441-449.
  • Miles, A.J., Whitmore, L., and Wallace, B.A. (2005) Spectral Magnitude Effects on the Analyses of Secondary Structure from Circular Dichroism Spectroscopic Data. Protein Science 14:368-374.
  • Wallace, B.A. (2005) Shining New Light on Protein Structure and Function thru Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy. Australian Biochemist 36: 47-50.
  • O'Reilly, A.O., Khambay, B.P.S., Williamson, M.S., Field, L.M., Wallace, B.A. and Davies, T.G.E. (2006) Modelling insecticide binding sites at the voltage-gated sodium channel. Biochemical Journal 396:255-263.
  • Whitmore, L., Janes, R.W., and Wallace, B.A. (2006) Protein Circular Dichroism Data Bank (PCDDB): Data Bank and Website Design. Chirality 18:426-429.
  • Wallace, B.A., Whitmore, L., and Janes, R.W. (2006) The Protein Circular Dichroism Data Bank (PCDDB): A Bioinformatics and Spectroscopic Resource. Proteins: Structure, Function and Bioinformatics 62:1-3.
  • Miles, A.J. and Wallace, B.A. (2006) Synchrotron Radiation Circular Dichroism Spectroscopy of Proteins and Applications in Structural and Functional Genomics. Chem. Soc. Reviews 35:39-51.
  • Lees, J.G., Miles, A.J., Wien, F., and Wallace, B.A. (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22:1955-1962.
  • Lees, J.G., Miles, A.J., Janes, R.W., Wallace, B.A. (2006) Optimisation and development of novel methodologies for secondary structure prediction from circular dichroism spectra. BMC Bioinformatics 7:507-517.
  • Evans, P., Bateman, O.A., Slingsby, C., and Wallace, B.A. (2007) A Reference Dataset for Circular Dichroism Spectroscopy Tailored for the BB-Crystallin Lens Proteins. Experimental Eye Research 84:1001-1008.
  • McKibbin, C., Farmer, N.A., Jeans, C., Reeves, P.J., Khorana, H.G., Wallace, B.A., Edwards, P.C., Villa, C., and Booth, P.J. (2007) Opsin Stability and Folding: Modulation by Phospholipid Bicelles. J. Mol. Biol. 374:1319-1332.
  • Miles, A.J., Hoffman, S.V., Tao, Y., Janes, R.W., and Wallace, B.A. (2007) Synchrotron radiation circular dichroism (SRCD) spectroscopy: New beamlines and new applications in biology, Spectroscopy 21:245-255.
  • Evans, P., Slingsby, C., and Wallace, B.A. (2008) Association of Partially-Folded Lens betaB2-Crystallins with the a-Crystallin Molecular Chaperone. Biochemical Journal 408:691-699.
  • Cowieson, N.P., Miles, A.J., Robin, G., Forwood, J.K., Kobe, B., Martin, J.L., and Wallace, B.A. (2008) Evaluating Protein: Protein Complex Formation using Synchrotron Radiation Circular Dichroism Spectroscopy. Proteins: Structure Function Bioinformatics 70:1142-1146.
  • Bulheller, B., Miles, A.J., Wallace, B.A., and Hirst, J. (2008) Charge-transfer transitions in the vacuum ultraviolet of protein circular dichroism spectra. J. Phys. Chem. B 112:1866-1874.
  • Whitmore, L., and Wallace, B.A. (2008) Protein Secondary Structure Analyses from Circular Dichroism Spectroscopy: Methods and Reference Databases. Biopolymers 89:392-400.
  • Miles, A.J., Drechsler, A., Kristan, K., Anderluh, G., Norton, R.S., Wallace, B.A. and Separovic, F. (2008) The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: a synchrotron radiation circular dichroism spectroscopic study. BBA (Biomembranes) 1778: 2091-2096.
  • Lampert, A., O'Reilly, A.O., Dib-Hajj, S.D., Tyrrell, L., Wallace, B.A., and Waxman, S.G. (2008) A pore-blocking hydrophobic motif at the cytoplasmic aperture of the closed-state Nav1.7 channel is disrupted by the erythromelalgia-associated F1449V mutation. J. Biol. Chem. 283:24118-24127.
  • Nurani, G., Radford, M., Charalambous, K., O'Reilly, A.O., Cronin, N., Haque, S., and Wallace, B.A. (2008) Tetrameric Bacterial Sodium Channels: Characterisation of Structure, Stability, and Drug Binding. Biochemistry 47:8114-8121.
  • O'Reilly, A.O., Charalambous, K., Nurani, G., Powl, A.M. and Wallace, B.A. (2008) G219S Mutagenesis as a Means of Stabilising Conformational Flexibility in the Bacterial Sodium Channel NaChBac. Molecular Membrane Biology 25: 670-676.
  • Charalambous, K., O'Reilly, A.O., Bullough, P., and Wallace, B.A. (2009) Thermal and chemical unfolding and refolding of a eukaryotic sodium channel. Biochim. Biophys. Acta (Biomembranes) 1788:1278-1286.
  • Drechsler, A., Miles, A.J., Norton, R.C., Wallace, B.A. and Separovic, F. (2009) Effect of Lipid on the Conformation of the N-Terminal Region of Equinatoxin II: A Synchrotron Radiation CD Study. European Biophysics Journal 39:121-127.
  • Wallace, B.A. (2009) Protein Characterisation by Synchrotron Radiation Circular Dichroism Spectroscopy. Quarterly Reviews of Biophysics 42:317-370.
  • Wallace, B.A. and Janes, R.W. (2010) Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy - An Enhanced Method for Examining Protein Conformations and Protein Interactions. Biochemical Society Transactions 38:861-873.
  • Kintzer, A.F., Sterling, H.J., Tang, I.I., Abdul-Gader, A., Miles, A.J., Wallace, B.A., Williams, E.R., and Krantz, B.A. (2010) Role of the protective antigen octamer in the molecular mechanism of anthrax lethal toxin stabilization in plasma. J. Mol. Biol. 399:741-758.
  • Powl, A.M., O'Reilly, A.O., Miles, A.M. and Wallace, B.A. (2010) Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly. Proc. Natl. Acad. Sci. (USA) 107: 14064-14069.
  • Zhai, J., Pattenden, L.K., Miles, A.J., Lee, T-H., Augustin, M.A., Wallace, B.A., Aguilar, M-I., and Wooster, T.J. (2010) Changes in beta-lactoglobulin conformation at the oil/water interface of emulsions studied by synchrotron radiation circular dichroism. Biomacromolecules 11: 2136-2142.
  • Klose, D.P., Wallace, B.A. and Janes, R.W. (2010) 2Struc: The Secondary Structure Server. Bioinformatics 26:2624-2625.
  • Meersman, F., Atilgan, C., Miles, A.J., Bader, R., Shang, W., Matagne, A., Wallace, B.A., and Koch, M.H.J. (2010) Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamics. Biophysical J. 99:2255-2263.
  • Whitmore, L., Woollett, B., Miles, A.J., Janes, R.W., and Wallace, B.A. (2010) The Protein Circular Dichroism Data Bank - A Web-based Site for Access to Circular Dichroism Spectroscopic Data. Structure 18:1267-1269.
  • Moore, B., Miles, A.J., Guerra-Giraldez, C., Simpson, P., Iwata, M., Wallace, B.A., Matthews, S.J., Smith, D.F., and Brown, K.A. (2011) Structural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane Surfaces. J. Biol. Chem. 286:9246-9256.
  • Wallace, B.A., Gekko, K., Hoffmann, S.V., Lin, Y-H., Sutherland, J.C., Tao, Y., Wien, F., and Janes, R.W. (2011) Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy - An Emerging Method in Structural Biology for Examining Protein Conformations and Protein Interactions. Nuclear Instrumentation and Methods A 649: 177-178.
  • Beich-Frandsen, M., Vecerek, B. Konarev, P.V., Sjoblom, B., Kloiber, K., Hammerle, H., Rajkowitsch, L., Miles, A.J., Kontaxis, G., Wallace, B.A., Svergun, D.I., Konrat, R., Blasi, U. and Djinovic-Carugo, K. (2011) S tructural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Research, 39:4900-4915.
  • Whitmore, L., Woollett, B., Miles, A.J., Klose, D.P., Janes, R.W., and Wallace, B.A.(2011) PCDDB: The Protein Circular Dichroism Data Bank, A Repository for Circular Dichroism Spectral and Metadata. Nucleic Acids Research 39:D480-D486.
  • McCusker, E.C., D'Avanzo, N., Nichols, C.G., and Wallace, B.A. (2011) Simplified Bacterial "Pore" Provides Insight into the Assembly, Stability and Structure of Sodium Channels. J. Biol. Chem. 286:16386-16391.
  • McCusker, E.C., Bagneris, C., Naylor, C.E., Cole, A.R., D'Avanzo, N., Nichols, C.G., and Wallace, B.A. (2012) Structure of a Bacterial Voltage-Gated Sodium Channel Pore Reveals Mechanisms of Opening and Closing. Nature Comms 3:1102.
  • O'Reilly, A.O., Eberhardt, E., Weidner, C., Alzheimer, C., Wallace, B.A., Lampert, A. 2012. Bisphenol A binds to the local anesthetic receptor site to block the human cardiac sodium channel. PLOS One 7:e41667
  • Erdmanis, L., O’Reilly, A.O., Williamson, M.S., Field, L.M., Turberg, A., and Wallace, B.A. (2012) Association of Neonicotinoid Insensitivity with a Conserved Residue in the Loop D Binding Region of the Tick Nicotinic Acetylcholine Receptor. Biochemistry 51: 4627-4629.
  • Powl, A.M., Miles, A.M., and Wallace, B.A. (2012) Transmembrane and extramembrane contributions to membrane protein thermal stability: studies with the nachbac sodium channel. Biochim. Biophys. Acta (Biomembranes) 1818:889-895.
  • Klose, D., Wallace, B.A., and Janes, R.W. (2012) DichroMatch: A website for similarity searching of circular dichroism spectra. Nucleic Acids Research 40:547-552.
  • Janes, R.W., Miles, A.J., Woollett, B., Whitmore, L., Klose, D., and Wallace, B.A. (2012) Circular Dichroism Spectral Data and Metadata in the Protein Circular Dichroism Data Bank (PCDDB): A Tutorial Guide to Accession and Deposition. Chirality 24: 751-63.
  • Woollett, B., Klose, D., Cammack, R., Janes, R.W., and Wallace, B.A. (2012) JCAMP-DX for circular dichroism spectra and metadata. Pure and Applied Chemistry 84: 2171-2182.
  • Ulmschneider, M.B., Bagneris, C., McCusker, E.C., DeCaen, P.G., Delling, M., Clapham, D.E., Ulmschneider, J.P. and Wallace, B.A. (2013) Molecular dynamics of ion transport through the open conformation of a bacterial voltage-gated sodium channel. Proc. Nat. Acad. Sci. (USA) 110, 6364-6369.
  • D'Avanzo, N., McCusker, E.C., Powl, A.M., Miles, A.J., Nichols, C.G., and Wallace, B.A. (2013) Differential Lipid Dependence of the Function of Bacterial Sodium Channels. PLOSone 8: e61216.
  • Lopes, J.L.S., Orcia, D., Araujo, A.P.U., DeMarco, R., and Wallace, B.A.(2013) Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). Biophysical J. 104:2512-2520.
  • Fernandez, D. I., Sani, M.–A., Miles, A. J, Wallace, B A, and Separovic, F. (2013) Membrane defects enhance the interaction of antimicrobial peptides, aurein 1.2 versus caerin 1.1. Biochimica et Biophysica Acta 1828: 1863–1872.
  • Woollett, B., Whitmore, L., Janes, R.W., and Wallace, B.A. (2013) ValiDichro: a website for validating and quality control of protein circular dichroism spectra. Nucleic Acids Research 41:W417-421.
  • Miles, A.J, Fedosova, N.U, Hoffmann, S.V., Wallace, B.A., Esmann, M. (2013) Stabilisation of Na,K-ATPase structure by the cardiotonic steroid ouabain. BBRC 435:300-305.
  • Bagneris, C., DeCaen, P.G., Hall, B.A., Naylor, C.E., Clapham, D.E., Kay, C.W.M., Wallace, B.A. (2013) Role of the C-terminal domain in the structure and function of tetrameric sodium channels, Nature Comms 4:2645.
  • O’Reilly, A.O., Cole, A.R., Lopes, J.L.S., Lampert, A., Wallace, B.A. (2013) Chaperone-mediated native folding of a B-scorpion Toxin in the periplasm of Escherichia coli. BBA (General Subjects) 1840:10-15.
  • Assuero F. Garcia; Jose L.S. Lopes; Antonio J. Costa-Filho; B. A. Wallace, Ana P.U. Araujo. (2013) Membrane Interactions of Calgranulin C (S100A12). PLOSone 8:e82555.
  • Kalsi, S. Powl, A.M. Wallace, B.A., Morgan, H., de Planque, M.R.R. (2014) Shaped apertures in photoresist films enhance the lifetime and mechanical stability of suspended lipid bilayers. Biophysical J. 106:1650-1659.
  • Bagneris, C., DeCaen, P.G., Naylor, C.E., Pryde, D., Nobeli, I., Clapham, D.E., & Wallace, B.A. (2014) The Prokaryotic NavMs Channel as a Structural and Functional Model for Eukaryotic Sodium Channel Antagonism. Proc. Natl. Acad. Sci. (USA) 111:.8428-8433.
  • Miles, A.J., Wallace, B.A. (2014) Circular Dichroism Spectroscopy for Protein Characterisation: Pharmaceutical Applications. In: Biophysical Characterization of Proteins in Developing Biopharmaceuticals. (Damian J. Houde and Steven A. Berkowitz, eds.) Elsevier Press.
  • O’Reilly, A.O., Williamson, M.S., Cabrera, J.G., Turberg, A., Field, L.M., Wallace, B.A., and Davies, T.G.E. (2014) Predictive 3D modelling of the interactions of pyrethroids with the voltage-gated sodium channels of ticks and mites. Pest Manag. Sci. 70:369–377
  • Ulmschneider, M.B., Ulmschneider, J.P. Schiller, N., Wallace, B.A., von Heijne, G., and White, S.H. (2014) Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion. Nature Comms. 5:4863
  • Lopes, J.L.S., Miles, A.J., Whitmore, L., and Wallace, B.A. (2014) Distinct circular dichroism spectroscopic signatures of polyproline II and unordered secondary structures: Applications in secondary structure analyses. Protein Science 23: 1765-1772
  • Perrone, B., Miles, A.J., Salnikov, E.S., Wallace, B.A., and Bechinger, B. (2014) Lipid interactions of LAH4, a peptide with antimicrobial and nucleic acid transfection activities. European Biophysics J. 43:499-507
  • Saha, S.C., Powl, A.M., Wallace, B.A., de Planque, M.R.R., Morgan, H. (2015), Screening ion-channel ligand interactions with passive pumping in a microfluidic bilayer lipid membrane chip. Biomicrofluidics 9:014103.
  • Amey, J.S., O’Reilly, A.O., Burton, M.J., Puinean, A.M., Mellor, I.R., Field, L.M., Wallace, B.A., Williamson, M.S. and Davies, T.G.E. (2015) An evolutionarily-unique heterodimeric voltage-gated cation channel found in aphids. FEBS Letters 589:598-607.
  • Lopes, J.L.S., Beltramini, L.M., Wallace, B.A. and Araujo, A.P.U. (2015) Deconstructing the DGAT1 Enzyme: Membrane Interactions at Substrate Binding Sites. PLosOne 10:e0118407
  • Saha, S., Henderson, A.J., Powl, A.M., Wallace, B.A., de Planque, M., Morgan, H. (2015) Characterization of the prokaryotic sodium channel NavSp pore with a microfluidic bilayer platform. PlosOne 10:e0131286
  • Bagneris, C., Naylor, C.E., McCusker, E.C., and Wallace, B.A. (2015) Structural Model of the Open-Closed-Inactivated Cycle of Prokaryotic Voltage-Gated Sodium Channels. J. Gen. Phys. 145:5-16.
  • W. C. Miller, A. J. Miles, B.A. Wallace (2016) Structure of the C-terminal Domain of the Prokaryotic Sodium Channel Orthologue NsvBa. Eur. Biophys. J. 45:807-814.
  • Naylor, C.E., Bagneris, C., DeCaen, P.G., Sula, A., Scaglione, A., Clapham, D.E. and B.A. Wallace. (2016) Molecular Basis of Ion Permeability in a Voltage-Gated Sodium Channel. EMBO J.  35:820-830.
  • Miles, A.J. and B.A. Wallace. (2016) Circular Dichroism Spectroscopy of Membrane Proteins. Chem. Soc. Rev. 45:4859-4872.
  • Penny, C.J., Rahman, T., Sula, A., Miles, A.J., Wallace, B.A*. Patel, S*. (2016) Isolated pores dissected from human two-pore channel 2 are functional. Scientific Reports 6:38426.
  • Colledge, M. and Wallace, B.A. (2017) A Webserver for Defining the Geometry of α-Helices in Membrane Proteins. Bioinformatics 33:1233-1234.
  • Sula, A., Booker, J., Ng, L., Naylor, C.E., DeCaen, P., Wallace, B.A. (2017) The complete crystal structure of an activated open sodium channel, Nature Comms. 8:14205.
  • Sula, A. and Wallace, B.A (2017). Interpreting the Functional Role of a Novel Interaction Motif in Prokaryotic Sodium Channels. J. Gen. Phys. 149:613-622.
  • O’Reilly, A.O., Lattrell, A., Miles, A.J., Klinger, A.B., Nau, C., Wallace, B.A. Lampert, A. (2017)  Mutagenesis of the NaChBac sodium channel discloses a functional role for a conserved S6 asparagine, Eur. Biophys. J. 46:665-674.
  • McDonald, C., Jovanovic, G., Wallace, B.A., Ces, O., and Buck, M. (2017) Structure and function of PspA and Vipp1 N-terminal peptides: insights into the membrane stress sensing and mitigation. Biochim. Biophys. Acta 1859:28–39.
  • Orcia, D., Zeraik, A., Lopes, J., Macedo, J., Santos, C., Oliveira, K., Anderson, L., Wallace, B.A., Verjovski-Almeida, S., Araujo, A., and DeMarco, R. (2017) Schistosoma mansoni MEG-14 interacts with human S100A9. Biochim. Biophys. Acta 1861:3490-3497.
  • Chin, S., Yang, D., Miles, A.J., Eckford, P.D.W., Molinski, S., Wallace, B.A. and Bear, C.E. (2017) Attenuation of phosphorylation-dependent activation of cysticfibrosis transmembrane conductance regulator (CFTR) by disease-causing mutations at the transmission interface. J. Biol. Chem. 292:1988–1999.
  • Field, L.M., Davies, T.G.E., O’Reilly, A.O, Williamson, M.S., Wallace, B.A. (2017) Voltage-gated sodium channels as targets for pyrethroid insecticide. Eur. Biophys. J. 46:675-679.
  • Yoneda, J.S., Miles, A.J., Araujo, A.P.U. and Wallace, B.A. (2017) Differential Dehydration Effects on Globular Proteins and Intrinsically Disordered Proteins during Film Formation. Protein Science 26:718–726.
  • Whitmore, L., Miles. A.J., Mavridis, L., Janes, R.W. and Wallace, B.A.(2017) PCDDB: New developments at the Protein Circular Dichroism Data Bank. Nucleic Acids Res. 45: D303–D307.
  • Whitmore, L, Mavridis, L, Janes, R.W., and Wallace, B.A. (2018) DichroMatch at the Protein Circular Dichroism Data Bank(DM@PCDDB): A Web-based Tool for Identifying Protein Nearest Neighbors using Circular Dichroism Spectroscopy.  Protein Science 27:10-13.
  • Tolchard, J., Walpole, S.J., Miles, A.J., Maytum, R.M., Eaglen, L.A., Hackstadt, T., Wallace, B.A., Blumenschein, T.M.A. (2018) The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix. Scientific Reports 8:1960.
  • Liko, I. Degiacomi, M. T.,  Lee, S., Newport, T., Gault, J., Reading, E., Hopper, J.T.S., Housden, N.G., White, P., Colledge, M., Sula, A., Wallace, B.A., Kleanthous, C., Stansfeld, P., Bayley, H., Benesch, J.L.P., Allison, T.M., and Robinson, C.V. (2018) Lipid binding attenuates channel closure of  the outer membrane protein OmpF. Proc. Natl. Acad. Sci. (USA) 115:6691-6696.
  • Kumagai, P.S., Gutierrez, R.F., Lopes, J.L.S., Martins, J.M., Jameson, D.M., Castro, A.M., Martins, L.F., DeMarco, R., Bossolan, N.R.S., Wallace, B.A., and Araujo, A.P.U. (2018) Acetomicrobium hydrogeniformans esterase (AhEst) displays high structural stability in extreme conditions. Extremophiles 22:781-793
  • Ke, S., Ulmschneider, M.B., Wallace, B.A.*, and Ulmschneider, J.P.* (2018) Role of the interaction motif in maintaining the open gate of an open sodium channel. Biophysical J. 115:1-11.
  • Ireland, S.M., Sula, A., and Wallace, B.A. (2018) Thermal Melt Circular Dichroism Spectroscopic Studies for Identifying Stabilising Amphipathic Molecules for the Voltage-Gated Sodium Channel NavMs.  Biopolymers 109:23067.
  • Miles, A.J., and Wallace, B.A. (2018) CDtoolX, a Downloadable Software Package for Processing and Analyses of Circular Dichroism Spectroscopic Data. Protein Science 27:1717-1722.
  • Montini, G., Booker, J., Sula, A., and Wallace, B.A. (2018) Comparisons of voltage-gated sodium channel structures with open and closed gates and implications for state-dependent drug design.  Biochemical Trans. 46:1567-1575.
  • Norman Davey et al. (2019) An Intrinsically Disordered Proteins Community for ELIXIR. F100Research.
  • Kumagai, P.S., Victor K. Sousa, V.K, Donato, M., Itri, R., Beltramini, L.M., Araujo, A.P.U., Buerck, J., Wallace, B.A.* and Lopes, J.L.S. (2019) Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. Eur. Biophys. J. 48:621–633. 
  • Miles, A.J. and B.A. Wallace. (2019) Biopharmaceutical Applications of Protein Characterisation by Circular Dichroism Spectroscopy (Houde, editor) Second Edition, in press.
  • Wallace, B.A. (2019) The Role of Circular Dichroism Spectroscopy in the Era of Integrative Structural Biology Curr. Opin. Structural Biology 58:191-196.
  • Zanatta, G., Sula, A., Miles, AJ., Ng, L., Torella, R., Pryde, D.C., DeCaen, P.G. and Wallace, B.A. (2019) Valproic Acid Interactions with the NavMs Voltage-Gated Sodium Channel, Proc. Natl. Acad. Sci. (USA) 116:26549-26554.

 

Our work is /has been supported by grants from the BBSRC, the EPSRC, the MRC, the Rosetree Trust, NIAA, NIH, IUPAC, Pfizer Neusentis, Bayer Animal Health, CNPQ (Brazil), the Heptagon Fund, EU Marie Curie Funding, and the Wellcome Trust.

Current Group Members

Postdocs: Dr. Andrew Miles, Dr. Altin Sula

PhD Students: Lily Goodyer Sait, Callum Haste, Niamh O'Malley, Declan Cook

Researchers:  David Hollingworth, Sergio Gomes Ramalli

 

Previous Lab Members (Partial List with Current Institutions)

PhD Students: David Mao, Donna Mielke (Argnonne National Lab, USA), Michael Cascio (Duquesne University, USA), Nancy [Swords]Jenny (University of Vermont, USA), Diane Peapus, Manju Venugopal, Declan Doyle (Univ. of Southampton), Chris Snook, Mark Richards (Leeds University), Andrias O’Reilly (Liverpool John Moores University), Y-C Chen (McKay Medical College, Taiwan), Paul Evans, Jonathan Lees (University College London), Jasveen Chugh (UCB Pharma), Sharmeen Haque (University College London), Matthew Radford, Neil Freeman (GSK), Andrew Orry (MolSoft), Timothy Stone (University of Cardiff, Wales), Ali Abdul-Gader (BioIVT), Ben Woollett, Graciella Cid, Toby Galbraith (Prime Global), Andrew Miles (Birkbeck),Wayne Miller (GSK), Alix Blockley (University of Leicester), Alex Henderson, Giulia Montini (Heptares), Jenny Booker (LeadPro), Matt Colledge (Actica Consulting), Elliot Drew (Queen Mary, University of London)
Postdocs:  Lee Whitmore (Simmore Software Ltd), Drew Woolley (University of Toronto, Canada), K. Ravikumar (University of Madras, India), Martha Kimball, Kalypso Charalambous (Kings College London), Nora Cronin (Inst. Cancer Res.), Andrew Powl, Andrias O’Reilly (Liverpool John Moores Univ.), Ghasem Nurani, Emily McCusker (Allergan), Claire Bagneris (Birkbeck), Claire Naylor (Molecular Dynamics), Oliver Smart (Anglia Ruskin Univ.), Frank Wien (Soleil Synchrotron), Maria Alvarez, Genacarlo Zanata (Federal University of Ceará) Brazil, Jose Luiz Lopes (University of Sao Paulo, Brazil), Juliana Yonada (Uinv. of Sao Paulo), Jose Luiz Lopes (Univ. of Sao Paulo, Brazil), Martin Ulmschneider (Kings College London)