Robert W. Janes
Senior Lecturer
School of Biological Sciences
Queen Mary
University of London
Mile End Road
London E1 4NS, U.K.
Fax: 44-(0)20-8983-0973
Email: r.w.janes@qmul.ac.uk
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
BOOK JUST PUBLISHED:
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
Research Interests
My
research interests are in the area of structural biochemistry with
emphasis on the investigations of the structure and function of
biologically
and medically important molecules, primarily using the techniques of X-ray
crystallography, nuclear magnetic resonance
and circular
dichroism.
I currently have a number of research projects
particularly
concerned with polypeptide toxins which selectively block ion
channels.
These include toxins against voltage-gated calcium, potassium, and
sodium
channels, as well as neuromuscular nicotinic acetylcholine receptors.
Controlled
administration of these toxins can have beneficial therapeutic actions.
For example peptomimetic drugs of calcium channel blocking toxins can
be
used as potential neuroprotectives, assisting in the treatment of
stroke
patients, as well as being anti-hypertensives, and having positive
inotropic
and anti-arrhythmic actions on the heart. We have recently solved the solution
structure of alpha-conotoxin SI a blocker of neuromuscular
nicotinic
acetylcholine receptors.
In a collaborative project with Prof.
Bonnie Wallace as part of studies at the BBSRC Centre for
Protein
and Membrane Structure and Dynamics (CPMSD)
we are undertaking pioneering work in developing the technique of Synchrotron
Radiation Circular Dichroism, carrying out proof of principle
experiments,
and determining the extent of the impact that this exciting extension
to
the more traditional laboratory-based CD experiments will have within
the
area of Biological Sciences, and Structural Genomics.
We have been collecting data for this work at the SRS
Daresbury, UK, ASTRID,
Aarhus, Denmark, and the NSLS,
Brookhaven, USA and will shortly be collecting on the new resource DIAMOND,
Oxford, UK.
Further research interests include aspects of bioinformatics,
notably structural modelling of novel proteins based on their sequence
and structure homology with other proteins.
In summary, my research into the structure/function
relationships
of biologically and medically important molecules is aimed towards a
better
understanding of their three dimensional conformations, which may
provide
useful information in aiding in the rational design of new drugs.
THE PROTEIN CIRCULAR DICHROISM DATA BANK
We
are announcing the creation of the Protein
Circular
Dichroism Data Bank (PCDDB).
Sponsorship for the pilot study from the BBSRC to B.A.
Wallace and R.W. Janes (Directors)
and L. Whitmore
(Developer)
is enabling the development of a prototype data bank. This is to
be a deposition data bank for the archiving and accession of Circular
and
Synchrotron Radiation Circular Dichroism Spectra of
biomacromolecules.
Included in the data bank facilities will be validation tools to enable
the checking of CD data prior to submission. We recently held a
meeting
of the International Scientific Advisory Board
to
comment on the proposed contents and design of the data bank, and on
validation
issues. An open consultation for comments on the concept of the
PCDDB,
and on its proposed contents, and the nature of the validation tools is
available by email to pcddb@mail.cryst.bbk.ac.uk.
Current Research Group Members
Dr. Daniel Klose (BBSRC Postdoc)
Former Research Group Members
Dr. Alison L. Cuff (BBSRC Postdoc)
Dr. Farah O'Boyle (Postgraduate Student)
Dr. Lee Whitmore (BBSRC Postdoc)
Dr. Jonathan Lees (BBSRC Postdoc)
Recent Selected Publications
- 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].
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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., 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.
- 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., 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.
- 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.
- 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. 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.
- 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.
- 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.
Last updated 13th July 2009
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