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,
Hsinchu, Taiwan, HiSOR,
Hiroshima, Japan, and at ANKA,
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.
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
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. We have also developed the DichroMatch
server 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. The major
structural biology resource we have created is
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
My research is supported by grants from the
Biotechnology and Biological Science Research Council
List of Current Research Collaborators
Wallace (Birkbeck College, University of London) Prof. Alison Roger (University of Warwick), Dr. Søren V.
Høffmann (ISA, Aarhus University) Prof. Wolfgang Laukau (Humboldt-Universität zu
Berlin), Dennis Nuernberg (School of Biological
and Chemical Sciences, Queen Mary, University of London)
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
(School of Biological and Chemical Sciences, Queen Mary, University of
Current Research Group Members
Mavridis (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
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.
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.
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.
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
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,
and Structure Comparisons with Related Analogs. J. Chem.
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.
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
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.
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].