APPENDIX 94
Memorandum from Dr Justin Molloy, National
Institute for Medical Reseach
INTERDISCIPLINARY
RESEARCH AT
MILL HILL
I am writing to you on behalf of scientists
at NIMR who trained in the physical sciences (including chemistry,
physics, mathematics and engineering) and who work at the interface
between classical scientific disciplines. We all believe that
interdisciplinary research is of critical importance in the post
genomic era of biomedical research. We also believe that interdisciplinary
research can continue to be conducted, effectively and in a world-leading
manner, at the National Institute for Medical Research based on
its current site at Mill Hill.
OUR MAIN
AREAS OF
RESEARCH ARE:
Mathematical Biology: De novo structure prediction,
bioinformatics, modelling of mesoscopic and complex systems.
Physical Biochemistry: Synthetic organic chemistry,
enzyme kinetics and mechanism, single molecule research, AFM,
CryoEM, optical tweezers, single molecule fluorescence imaging
in cells, mechanistic studies of motor proteins, DNA processing
enzymes, signalling molecules and membrane receptors, medical
nanotechnology.
Protein Structure: X-ray crystallography structure
determination, enzyme mechanism, protein complex assembly
Molecular structure: NMR structure determination
and molecular dynamics, biomolecular interactions and the MRC
Biomedical NMR centre.
BACKGROUND
(1) We have an excellent track record of
interdisciplinary research: work from the Divisions of Physical
Biochemistry, Mathematical Biology, Protein Structure, Molecular
Structure and the MRC Biomedical NMR centre is world-leading and
the scientific excellence of our work has never been in question.
We believe that the breadth and quality of the interdisciplinary
work we do, reflects the fact that the research programmes have
evolved organically over the past 20 years. Mill Hill is unique
in the UK in that there are genuinely no scientific barriers here
and this is what draws the best young people to work here.
(2) We can still recruit the best scientists
doing interdisciplinary science to NIMR. Over the past two years
we have recruited Molloy & Veigel (single molecule research),
Goldstein (mathematical and systems biology), Rosenthal (cryo-electron
microscopy), Ramos and Driscoll (molecular structure and NMR).
We must be doing something right in order to out-compete Cambridge,
Oxford, Imperial and several other leading UK Universities to
recruit such people to work here.
(3) Significantly, we have also retained
all senior staff that work in this area in spite of tempting offers
being made to induce them to move elsewhere. Staff morale remains
high: we are passionate about the NIMR, loyal to MRC but still
convinced that Mill Hill remains the best future site for the
renewed National Institute for Medical Research. We want our opinions
to be heard and do not wish to align ourselves with any dictum
that we think is flawed.
THE FUTURE
OF INTERDISCIPLINARY
SCIENCE AT
NIMR
We first want to dispel the misconception that
interdisciplinary work at Mill Hill cannot continue to thrive
here in the future. Our vision for interdisciplinary research
at Mill Hill is forward-looking and is based on a "tried-and-tested"
plan. The future of interdisciplinary science maintained on the
current site at the Mill Hill site would involve no compromises.
This is in sharp contrast to the proposed moves to central London
that involve fragmenting the science because of conflicting demands
of our work in terms of space, vibration and magnetic fields.
It would be unacceptable to break up the interdisciplinary community
that has been created in Mill Hill and madness to hive it off
from the rest of the Institute. Furthermore, Mill Hill is on a
secure site where our highly quantitative work can be translated
readily into animal models and used to study live cells and genetically
manipulated organisms.
Mill Hill has massive scope for expansion and
since funding for biomedical research will increase over the next
20 years (as part of our new knowledge-based economy), the MRC
will need to expand both its extramural and its intramural research
capacity. Mill Hill offers a single contiguous site, with ample
space for expansion, and this will enable us to compete with the
best in the USA, Japan, Germany, France and Scandinavia. Interdisciplinary
work often has special infrastructure needs and Mill Hill provides
the necessary flexibility in this respect.
We are sympathetic with our University colleagues
who face significant barriers and problems in embracing interdisciplinary
research. These include, geographically separated departments,
intellectual isolation between communities, problems in juggling
teaching commitments and research, poor uptake of physical science
undergraduate courses, difficulties in organising interdisciplinary
graduate and undergraduate taught courses and poor "matchmaking"
between the best biologists and the best physical scientists.
Moving NIMR to UCL or King's is unlikely to help or alleviate
any of these problems. The short-term political and financial
impact might be significant (eg RAE 2007). However, the long-term
scientific benefit to the "host" University in terms
of boosting interdisciplinary research might only be marginal
at best.
We fear plans to move NIMR to King's or UCL
might damage our research capacity: Both of the proposed new sites
will be spatially constrained and future expansion will be limited.
The Institute may need to be geographically fragmented in order
to facilitate the conflicting needs of physical science work (involving
high-field NMR, low vibration requirements for cryo-EM and single
molecule research). This factor alone will destroy our vision
for interdisciplinary research remaining a completely integrated
component of the Institute. Staff recruitment to a central London
location will also be difficult or prohibitively expensive.
We know that over the next 10-20 years, interdisciplinary
research will permeate all aspects of biomedical research from
molecules to cells and from cells to organisms. On this point,
we believe that the contentious issue of where to place the animal
house is being unrealistically "glossed-over". We know
that there will be huge knock-on problems in terms of security
and ease of access across the institute if the animal facility
were to be located within central London.
We have a clear view of how our science will
develop in the future and we have prepared a case for how this
can be achieved at Mill Hill. However, we wonder why the MRC Council
fear our bid so much that they refuse to consider it alongside
the King's and UCL bids as an equal "Option". We simply
do not understand the political complexity and wonder why our
views and our vision are being compromised and marginalized. We
actually wonder whether we are the people whom MRC intend to recruit
to staff the renewed NIMR.
We would welcome the opportunity to engage fully
with MRC Council to help develop interdisciplinary research at
NIMR. For a secure and successful future, we would like there
to be a continuing dialogue between our Director and staff at
NIMR with MRC Council and Head Office.
|
Name | 1º/2º Degree
| Research Area | Speciality
|
|
Justin Molloy | Physiology/
Biophysics
| Molecular Biophysics | Single Molecules, nanotechnology
|
Claudia Veigel | Medicine Biochemistry MD/PhD
| Molecular Biophysics | Single Molecules, nanotechnology
|
Martin Webb | Chemistry |
Biochemistry | Molecular Mechanism
|
John Eccleston | Chemistry |
Biochemistry | Molecular Mechanism
|
John Corrie | Chemistry |
Organic Synthesis | Molecular Probes
|
Edward Hulme | Biochemistry
| Membrane Proteins | Structure of GPCRs
|
Nigel Birdsall | Chemistry |
Pharmacology | GPCR pharmacology
|
Peter Rosenthal | Physics |
Electron microscopy | Single particle cryo-EM, molecular structure determination, cell tomography
|
Lesley Calder | Biology |
Electron Microscopy | High Resolution, negative stain EM
|
Peter Bayley | Physics |
Molecular Biophysics | Biomolecular interactions
|
Mark Wallace | Chemical Physics
| Biological Fluorescence | Single Molecules, nanotechnology
|
Stephan Schmitz | Biotechnology
| Molecular biophysics | Optical tweezers, motor proteins
|
Gregory Mashanov | Physiology
Biophysics
| Cell Biophysics | Cell biology, single molecules, computer programming, nanotechnology
|
Gordon Reid | Chemistry |
Organic Synthesis | labelled nucleotides
|
Peter Fletcher | Chemistry |
Peptide synthesis | Peptide synthesis
|
Steve Martin | Chemistry |
Molecular Biophysics | Optically based biophysics, biomolecular interactions
|
Mike Anson | Physics | Molecular Biophysics
| Optically based studies of single motor proteins
|
George Papageorgio | Chemistry
| Organic Synthesis | Molecular probes/caged compounds
|
Ranjit Munasinge | Chemistry
| Organic Synthesis | Molecular probes/caged compounds
|
Mark Dillingham | Biochemistry
| Protein-DNA interactions | Structure-function determination of DNA helicases
|
Michael Okoh | Biochemistry
| Small molecule probes | Cell-based assays of inorganic phosphate
|
Richard Goldstein | Mathematics
| Mathematical Biology | Bioinformatics, systems biology
|
Willie Taylor | Mathematics
| Mathematical Biology | Structures-function, bioinformatics, complexity mesoscopic systems.
|
Fernandez Reyes | Details to follow
| Mathematical Biology | Bioinformatics, systems biology
|
Douglas | Details to follow
| Mathematical Biology | Bioinformatics, systems biology
|
Saldanha | Details to follow
| Mathematical Biology | Bioinformatics, systems biology
|
Blackburne | Details to follow
| Mathematical Biology | Bioinformatics, systems biology
|
Sheth | Details to follow |
Mathematical Biology | Bioinformatics, systems biology
|
Chernova | Details to follow
| Mathematical Biology | Bioinformatics, systems biology
|
Michael Green | Details to follow
| Mathematical Biology | Molecular modelling, MD simulations
|
Franca Fraternali | Details to follow
| Mathematical Biology | Molecular modelling, MD simulations
|
Guy Dodson | Chemistry
Physics
| X-ray Crystallography | Protein structure determination
|
Steve Smerdon | Genetics
Chemistry
| X-ray crystallography | Protein structure-function determination
|
Steve Gamblin | Biochemistry
| X-ray crystallography | Protein structure-function determination
|
Katrin Rittinger | Chemistry
| X-ray crystallography | Protein structure-function determination
|
Ian Taylor | Biochemistry
Biophysics
| X-ray crystallography | Protein structure-function determination
|
Phil Walker | Biochemistry |
X-ray crystallography | Protein crystallography, computing
|
Ennis-Adeniran | Biology
Biochemistry biophysics
| X-ray crystallography | Protein crystallography
|
Lloyd | Biology
Biochemistry biophysics
| X-ray crystallography | Protein crystallography
|
Xiao | Biology
Biochemistry biophysics
| X-ray crystallography | Protein crystallography
|
Smith | Biology
Biochemistry biophysics
| X-ray crystallography | Protein crystallography
|
Dutta | Biology
Biochemistry biophysics
| X-ray crystallography | Protein crystallography
|
Steven Howell | Biochemistry
Mass Spec.
| Mass Spectrometry | Protein-ligand Mass Spec. MALDI TOF
|
Dan Zhu | Computer Science |
Bioimaging/optical techniques. Computation |
Computer programming, algorithm development image analysis
|
Stamatis Pagakis | Electrical Engineering Biomedical Engineering
| Bioimaging/optical techniques | Imaging methods, including method develoment, image analysis. Cellular and molecular imaging
|
Annalisa Pastore | Biochemistry
| Nuclear Magnetic Resonance Spectroscopy |
Molecular structure determination, protein-ligand, protein-protein interactions
|
Tom Frenkiel | Physics NMR |
NMR | MRC Biomedical NMR facility
|
Geoff Kelly | NMR | NMR
| MRC Biomedical NMR facility |
Andres Ramos | Biology Biophysics
| NMR | Molecular Structure determination, protein-ligand, protein-protein interactions.
|
Adolfini | Biology | NMR
| Molecular Structure determination |
Jake Grimmett | Biology
Biology-computing
| NMR | Computing/computer programming/ Algorithm development
|
McCorrmick | Biology | NMR
| Molecular Structure determination |
Birdsall | Biology | NMR
| Molecular interactions |
Laura Masino | Biochemistry
Biophysics
| NMR | Protein structure-function relationships
|
Hollingworth | Biochemistry
| NMR | |
Bliss | Physics & Physiology
Physiology
| Long-term potentiation and memory |
|
Ogden | Biology
Electrophysiology
| Electrophysiology of sensory cells and hippocampal slices
| Two-photon photolysis of caged compounds in synaptic clefts.
|
|
23 November 2004 | |
| |
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