Robert W. Janes

Senior Lecturer
School of Biological & Chemical Sciences
Queen Mary
University of London
Mile End Road
London E1 4NS, U.K.
Fax: 44-(0)20-8983-0973

B.Sc. (Chemistry, Royal Holloway College, University of London)
M.Sc. (Crystallography, Birkbeck College, University of London)
Ph.D. (Crystallography, Birkbeck College, University of London)
Fellow, Royal Society of Chemistry
Fellow, International Union of Pure and Applied Chemistry


"Modern Techniques for Circular Dichroism and Synchrotron Radiation Circular Dichroism Spectroscopy"

B.A. Wallace and R.W. Janes, Editors

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Research Interests

Crystal structure of alpha-conotoxin SI with a
        superimposition of the backbone secondary structure

My research interests are in the area of structural biology and bioinformatics, particularly in the development of new methods and tools to enable and develop the important technique of Circular Dichroism (CD) spectroscopy and the newly emerging method of Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy.  In a collaborative project with Prof. B.A. Wallace as part of studies initiated at the BBSRC Centre for Protein and Membrane Structure and Dynamics (CPMSD) [for which I have been a member of the Advisory Board for many years], I have undertaken proof of principle experiments, instrumentation design and the development of new applications of SRCD to anwer questions of biological importance.  We have been involved in data collection and developmental projects at many synchrotrons,originally at the SRS Daresbury, UK and the NSLS, Brookhaven, USA, and now at ASTRID, Aarhus, Denmark, BSRF, Beijing, China, SOLEIL, Saint-Aubin, France, NSRRC, Hsinchu, Taiwan, HiSOR, Hiroshima, Japan, and at ANKA, Karlsruhe, Germany, where the original beamline CD12 from the SRS at Daresbury is now installed.

Through a number of collaborations, I am involved in projects utilising SRCD spectroscopy to provide answers to key questions in many areas of science including genetic diseases, medicine, dentistry, photosynthesis and biotechnology.

The Protein Circular Dichroism Data Bank

Another major focus of my lab has been in the area of Bioinformatics, developing new methods and tools for Structural Biology.  We have created the web-based server 2Struc that includes the "2Struc" methodology to enable calculations of the secondary structures present in a protein based on its atomic coordinates (PDB file), and the "Compare-the-Protein" functionality which allows the user to compare the secondary structures of pairs of proteins or within a group of NMR structures. The major structural biology resource we have created is the Protein Circular Dichroism Data Bank (PCDDB), a highly-used international facility, which is a publicly-accessible deposition database for data sharing and access to CD spectroscopic and metadata.  Included as part of the data bank facilitiy is Validichro, a tool to enable the validation and establishing of community standards for spectroscopic data.
We have also developed the DichroMatch server (now part of the PCDDB) for identification of a protein's structure and function based on its CD spectrum, which also has applications in bioprocessing and biosimilar comparisons for pharmaceutical applications.  Our recent CD package that we have available is PDB2CD, which can be used to generate CD (SRCD) spectra from atomic coordinates from a PDB format file.

My research is supported by grants from the Biotechnology and Biological Science Research Council

List of Current Research Collaborators

Prof. B.A. Wallace (Birkbeck College, University of London)
Prof. Alison Roger (University of Warwick), Dr. Søren V. Høffmann (ISA, Aarhus University, Denmark)
Prof. Wolfgang Laukau (Humboldt-Universität zu Berlin, Germany)
Dr. Paul Anderson (School of Medicine and Dentistry, Queen Mary, University of London)

Dr. Robin Maytum (University of Bedfordshire)
Dr. Norbert Krauss, Dr. Kristina Zubow (Karlsruhe Institute of Technology, Germany)

Current Research Group Members

Elliot Drew (BBSRC Postdoc)

Former Research Group Members

Dr. Andrew Benie (Postgraduate Student)

Dr. Alison L. Cuff  (BBSRC Postdoc)
Dr. Farah O'Boyle  (Postgraduate Student)
Dr. Lee Whitmore (BBSRC Postdoc)
Dr. Jonathan Lees (BBSRC Postdoc)
Dr. Daniel Klose  (BBSRC Postdoc)
Dr. Benjamin Woollett  (BBSRC Postdoc)
Dr. Lazaros Mavridis  (BBSRC Postdoc)

Recent Selected Publications

  • 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. [selected as Featured Article by NAR Editor – top 5% in journal based on originality, significance and scientific excellence]
  • Wallace, B.A., Gekko, K., Vronning Hoffmann, 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 Instruments & Methods in Physics Research Section A-Accelerators Spectrometers Detectors and Associated Equipment. 649:177-178.
  • 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.
  • Klose, D.P., Wallace, B.A. and Janes, R.W. (2010) 2Struc: The Secondary Structure Server. Bioinformatics 26:2624-2625.
  • Wallace, B.A. and Janes, R.W. (2010) Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy: an enhanced method for examining protein conformations and protein interactions. Biochem. Soc. Trans. 38:861-873.
  • Lees, J.G. and Janes, R.W. (2008) Combining Sequence-Based Prediction Methods and Circular Dichroism and Infra-Red Spectroscopic Data to Improve Protein Secondary Structure Prediction. BMC Bioinformatics 9:24
  • Miles, A.J., Janes, R.W., Brown, A., Clarke, D.T., Sutherland, J.C., Tao, Y., Wallace, B.A. and Hoffmann, S.V. (2008) Light Flux Density Threshold at which Protein Denaturation is Induced by Synchrotron Radiation Circular Dichroism Beamlines. Journal of  Synchrotron Radiation 15:420-422.
  • Miles, A.J., Hoffmann, 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. [cover article]
  • 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.
  • Lees, J.G., Miles, A.J., Janes, R.W. and Wallace, B.A. (2006) Novel Methods for Secondary Structure Determination Using Low-wavelength (VUV) Circular Dichroism Spectroscopic Data. BMC Bioinformatics 7:507. [designated as highly accessed]
  • 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.
  • Janes, R.W. (2005) Bioinformatics Analyses of Circular Dichroism Protein Reference Databases. Bioinformatics 21:4230-4238.
  • Janes, R.W. (2005) Alpha-conotoxins as selective probes for nicotinic acetylcholine receptor sub-classes. Current Opinion in Pharmacology 5:280-292.
  • Janes, R.W. and Cuff, A.L. (2005) Overcoming Protein Denaturation Caused by Irradiation in a High-Flux Synchrotron Radiation Circular Dichroism Beamline. Journal of Synchrotron Radiation 12:524-529.
  • Hawkes, N.J., Janes, R.W., Hemingway, J. and Vontas, J. (2005) Detection of Resistance-Associated Point Mutations of Organophophate-Insensitive Acetylcholinesterase in Olive Fruit Fly, Bactrocera oleae (Gmelin). Pesticide Biochemistry and Physiology 81:154-163.
  • Miles, A.J., Wien, F., Lees, J.G., Rodger, A., Janes, R.W. and Wallace, B.A. (2003) Calibration and Standardisation of Sycnchrotron Radiation Circular Dichroism and Conventional Circular Dichroism Spectrophotometers. Spectroscopy 17:653-661.
  • Wallace, B.A., Lees, J, Orry, A.J.W., Lobley, A. and Janes, R.W. (2003) Analyses of Circular Dichroism Spectra of Membrane Proteins. Protein Science 12:875-884.
  • Janes, R.W. (2003) Nicotinic Acetylcholine Receptors:  Alpha-Conotoxins as Templates for Rational Drug Design. Biochem. Soc. Trans. 31:633-635.
  • Wallace, B.A. and Janes, R.W. (2003) Circular Dichroism and Synchrotron Radiation Circular Dichroism Spectroscopy:  Tools for drug discovery. Biochem. Soc. Trans. 31:630-632.
  • Wallace, B.A. and Janes, R.W. (2001) Synchrotron Radiation Circular Dichroism Spectroscopy of Proteins:  Secondary Structure, Fold Recognition and Structural Genomics.  Curr. Opin. Chem. Biol. 5:567-571.
  • Janes, R.W., Potter, B., Everett, S.A., Naylor, M.A., Stratford, M.R.L., and Wardman, P. (2001) 1-Methylindole-3-carboxaldehyde oxime derivatives. Acta Cryst C57:58-61.
  • Benie, A.J., Whitford, D., Hargitai, B., Barany, G. and Janes, R.W. (2000) Solution Structure of Alpha-Conotoxin SI. FEBS Letters 476:287-295.
  • Janes, R.W., Whitford, D., Benie, A., Hargittai, B. and Barany, G. (2000) Structural Studies on Alpha-Conotoxin SI. in 'Peptides for the New Millenium'. Proceedings of the 16th American Peptide Symposium. pp730-732.
  • Wallace, B.A. and Janes, R.W. (1999) Tryptophan in Membrane Proteins: X-ray Crystallographic Analyses. Adv. Exp. Med. Biol. 467:789-799.
  • Janes, R.W. (1999) Crystal Structure of an Analog of the Anticonvulsant Lamotrigine, 3,5-Diamino-6-(2,3,5-Trichlorophenyl)-1,2,4-Triazine�Dimethanolate, and Structure Comparisons with Related Analogs. J. Chem. Cryst. 29:163-167.
  • Rodi, D.J., Janes, R.W., Sangasnee, 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. Biol. 285:197-204.
  • Wallace, B.A. and Janes, R.W. (1999) Structure, Function, and Modeling of Human Endothelin and its Precursor Polypeptide, BigET: Targets for Rational Drug Design. Frontiers in Peptide Science, 15:358-360.
  • Janes, R.W., Munroe, P.B., Mitchison, H.M, Gardiner, R.M., Mole, S.E. and Wallace, B.A. (1996) A Structural Model for Batten Disease Protein CLN3: Functional Implications from Homology and Mutations. FEBS Letters 399:75-77.
  • Peto, H. Corder, R., Janes, R.W. and Wallace, B.A. (1996) A Molecular Model for Human BigEndothelin-1 (BigET-1). FEBS Letters 394:191-195.
  • Peishoff, C.E., Janes, R.W. and Wallace, B.A. (1995) Comparison of the Structure of the Endothelin A Receptor Antagonist BQ123 and N-Methyl Leucine BQ123 with the Crystal Structure of the C-Terminal Tail of Endothelin. FEBS Letters 374:379-383.
  • Wallace, B.A., Janes, R.W., Bassolino, D.A. and Krystek Jr., S.R. (1995) A Comparison of X-Ray and NMR Structures for Human Endothelin-1. Protein Science 4:75-83.
  • Janes, R.W. and Wallace, B.A. (1994) Modelling the Structures of the Isoforms of Human Endothelins Based on the Crystal Structure of Human Endothelin-1. Biochem. Soc. Trans. 22:1037-1043.
  • Janes, R.W., Peapus, D.H., and Wallace, B.A. (1994) Crystal Structure of Human Endothelin. Nature Structural Biology 1:311-319. [This paper was the subject of a News and Views Article, in Nature 369, 84].

  • Last updated 7th March 2018
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