Dr Neil Kad
Senior Lecturer in Molecular Biophysics
- 01227 (8)16151
In my lab we use single molecule techniques to understand the physical basis of how proteins interact.
A number of diseases are linked to alterations in these physical parameters and we aim to find solutions to these problems.
- DNA Repair
- Muscle Contraction
- Neurodegenerative Disease
We have been funded by the BBSRC, Parkinson's UK, British Heart Foundation, Royal Society and the STFC.
Neil Kad joined the School of Biosciences in August 2014, his previous positions were:
- 2007-2014 – Lecturer, Department of Biological Sciences, University of Essex
- 2004-2007 – Research Associate (PI: Prof. DM. Warshaw), Department of Molecular Physiology and Biophysics, University of Vermont, Vermont USA.
- 2001-2004 - Postdoctoral Research Associate (PI: Prof. DM. Warshaw), Department of Molecular Physiology and Biophysics, University of Vermont, Vermont USA.
- 1998-2001 – Postdoctoral Research Associate (PI: Prof. SE. Radford), Department of Biochemistry, University of Leeds, Leeds UK.
- 1994-1998 - Ph.D. in the conformational kinetics of the chaperonins GroEL and GroES (PI: Prof. AR. Clarke). Department of Biochemistry, University of Bristol
- 1991-1994 - B.Sc. (Hons) Biochemistry. University of Sheffield
Investigating the function of motile enzymes on their tracks. I have two main research foci, the first involves looking at DNA repair and the second myosin function. The latter is the motor enzyme responsible for a number of cellular tasks from muscle contraction to cargo transport.
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Also view these in the Kent Academic Repository
My key research areas are:
- DNA repair
- Single Molecule Biophysics
- Muscle Contractility
- Amyloid disease and inhibition
- Molecular Motors
To study these enzymes we use single molecule techniques, in particular Fluorescence Microscopy and a technique called tightroping, where we suspend nanowires of DNA or actin between surface immobilised pedestals (fig1)
We label our proteins with quantum dots, these are small nanocrystals that fluoresce brightly and are extremely resistant to photobleaching, making them ideal tools in the study of biological processes.
Using these approaches we are able to shed light on how the enzymes involved in DNA repair interact with one another and with their DNA substrate.
In addition, we have been able to show how myosin's function is coupled to load, and also how myosin's function is related to its structure.
Finally we are really interested in advanced technologies for probing single molecules, such as the use of nanoprobes in collaboration with the Rutherford Appleton Labs in Harwell.
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- Stage 1
Enzymes and Introduction to Metabolism