Dr. Beth Bromley
Lecturer in Soft Matter and Biological Physics
Dr. Bromley is an early career scientist. She completed an undergraduate degree in Natural Sciences in Cambridge and then her PhD with Prof. Athene Donald F.R.S. on the self-assembly and structure formation of the protein beta-lactoglobulin. She then secured a MRC discipline hopping grant to work with Prof. Carol Robinson FRS on the fibrillogenesis of amyloidogenic peptides by nano-spray ESI mass spectrometry and then a PDRA position to work with Prof. Dek Woolfson in Bristol on the design and fabrication of self-assembling peptides. Dr. Bromley has worked with some the very best senior staff in Soft Matter and Biophysics the UK.
She has world-class expertise in computational and experimental biophysical techniques for designing, fabricating and characterising biomolecular and self-assembling systems. She has research expertise in the flow of starch granules, structure formation in self-assembling milk proteins amyloid fibre formation, subunit exchange in amyloidogenic proteins, alpha-helical fibre formation, specificity of protein-protein interactions and the design of protein based nanostructures.
Lara is an EPSRC funded PhD student. Her project involves the synthesis of designed coiled coil peptides that assembly into discrete nano-structures. Once these structures have self-assembled, their structure and dynamics are investigated using a range of techniques including UV and CD spectroscopy, Fluorescence Lifetime and Anisotropy as well as Dynamic light scattering and FRET.
Asahi is an EPSRC funded PhD student. His project involves the synthesis of synthetic amino acid analogues for metal binding. These novel amino acids will be incorporated into self-assembling peptide systems in an attempt to form both novel metal based catalysts but also in order to investigate to what extent the self-assembly can control metal binding and to what extendt the metal binding can control self-assembly. The project is in collaboration with Dr. steve Cobb and Dr. Corrina Hess.
David did a 4th year research project in the group on examining the properties of peptides that were designed to switch between a random coil and helical conformation. He found that sequence was indeed a key parameter in determining whether a peptide could be switched between the two states as a function of redox potential.
Richard did a 4th year research project in the group investigating the fluorescence lifetime and anisotropy of labelled alpha-helical coiled coils. He found that the tumbling rate of the coiled coils in solution was faster than any measurable global vibrational modes of the coiled coil structure and hence was unable to measure any such modes.
Mohan did a 4th year research project in the group continuing from the previous project carried out by Mike in investigating the dissociation rates of desinged coiled coils using dual polarisation inteferometry in collaboration with Dr. Graham Cross. He found that the dissociation behaviour of the coiled coils was extremely complex and that binding appeared to be unexpectedly irreversible in some cases.
Arin did a 4th year research project in the group, creating fluorescently labelled coiled coil peptides for examination using FRET and fluorescence lifetimeand anisotropy experiments. She is now studying for a Ph D in the Atmol group in Durham.
Mike did a 4th year research project in the group, making synthetic coiled coil proteins for testing in dual polarization interferometry in collaboration with Dr. Grahm Cross.
Reuben did a 4th year research project in the group, followin gon from Alan's work and completing the algorithm to find sequence fragments that adopt different stuctures in different contexts. He found several interesting sequences that had been crystallised in utterly different conformations.
Alan did a Nuffield summer studentship in the group, writing software to extract information about sequences that adopt multiple different structures and designing peptide sequences that would define regions of structural change, for example form the end of beta-sheet and the beginning of an alpha helix.
Professor Durham University
Tom McLeish is a Professor of Soft condesed matter and biological physics at the Durham University. His research interests include thermal motion, statistical mechanics and noise in biological processes. With biologists and biochemists his group are unravelling allosteric signalling in proteins and processes in amyloid fibril assembly. He has advocated a high-dimensional view of protein folding, and a “genotype-phenotype” model of evolutionary landscapes
Lecturer Durham University
Dr. Cobbs group uses a range of methods and techniques in synthetic organic and peptide chemistry to tackle interesting and challenging biological problems. Some project highlights include: New antiparasitics inspired by naturally occurring antimicrobial peptides, peptide inhibitors of chemokine induced chemotaxis are being designed, with the aim of reducing inflammation and thus protecting cardiac tissue during heart by-pass operations, new biomaterials and light activated peptide drug delivery systems that exploit novel amino acids, utilising Solid Phase Peptide Synthesis (SPPS) novel amino acids probes prepared within the group.
Lund University, Sweden
Heiner Linke is a Professor of Nano physics and deputy director of the Nanometer Structure Consortium, comprising 100 scientists covering research ranging from Materials Science and Quantum Physics to applications in the areas of Electronics, Photonics and the Life Sciences. His research group uses experimental and numerical methods to study transport phenomena far from thermal equilibrium. One focus is on nanoelectronic systems, where they investigate non-linear quantum transport phenomena, symmetry breaking, and efficient thermoelectric power conversion. They also develop artificial protein motors, study the interaction of protein motors with nanostructures, and explore fluid motion driven by ratchet phenomena. A common theme of these research projects is the physics of ratchets and Brownian motors: the interplay of nonequilibrium, asymmetry, and thermal motion to create directed transport.
Simon Fraser University, Canada
Nancy Forde is a professor in the physics department of SFU. Her group probe the single-molecule mechanical properties of collagen and elastin using optical tweezers; characterize the viscoelasticity of solutions and networks using optical tweezers based microrheology; and are developing holographic optical tweezers to measure the stress-strain behaviour of networks on the microscale.
University of New South Wales, Australia
Paul Curmi is a professor of biophysics in the physics department of the UNSW. He is interested in the structure of biological macromolecules, especially proteins. In order to understand the complex processes that occur in living systems it is essential to know the atomic structures of the macromolecules responsible for the processes. His research covers: the determination of protein structure; examining the physical properties of proteins; and determining the relationship between protein structure and sequence.
University of Bristol, UK
Dek Woolfson is a professor of Chemistry and Biochemistry and holds a joint chair in chemistry and biochemistry at the University of Bristol. The primary basic research interest of the group is the informational aspect of the protein-folding problem; that is, how does the sequence of a protein determine its active, three-dimensional structure or fold? We tackle this problem using the following multi-disciplinary approach: We use bioinformatics to garner sequence-to-structure relationships from protein sequence and structural databases. We test the relationships ("rules for protein folding") that we find in two ways: (a) through ab initio protein-structure prediction; and (b) via rational protein design, where we engineer natural protein structures, or design new ones completely from scratch (so-called de novo design). We then test our engineered and design proteins experimentally using biophysical methods. The peptides and proteins are made either by peptide synthesis, or via recombinant DNA methods and the expression of synthetic genes. The products and then characterised using methods including: solution-phase biophysics (CD, FT-IR and fluorescence spectroscopy, AUC and ITC); high-resolution structural biology (NMR spectroscopy and X-ray crystallography); and microscopy (EM, AFM and light microscopy). Finally, we explore potential applications of some the engineered and designed proteins in the burgeoning fields of bionanotechnology and synthetic biology.