Professor Neil Kad

Professor Neil Kad's lab uses 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 they aim to find solutions to these problems:

• DNA Repair
  
• Muscle Contraction
• Neurodegenerative Disease 
  

The lab has been funded by the BBSRC, Parkinson's UK, British Heart Foundation, the Royal Society and the STFC. For further information, see Kad Lab.

Neil Kad joined the School of Biosciences in August 2014. His previous positions include: 

• 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. 

Neil's key research areas are: 

• DNA repair 
• Single Molecule Biophysics 
• Muscle Contractility Amyloid disease and inhibition 
• Molecular Motors 

To study these enzymes, he uses single molecule techniques, in particular Fluorescence Microscopy and a technique called tightroping, where you suspend nanowires of DNA or actin between surface immobilised pedestals.

The proteins are labelled with quantum dots; small nanocrystals that fluoresce brightly and are extremely resistant to photobleaching, making them ideal tools in the study of biological processes.

Using these approaches, he is able to shed light on how the enzymes involved in DNA repair interact with one another and with their DNA substrate. He has also been able to show how myosin's function is coupled to load, and how myosin's function is related to its structure.

Finally, Neil is interested in advanced technologies for probing single molecules, such as the use of nanoprobes in collaboration with the Rutherford Appleton Labs in Harwell.

Stage 1 

• BI301 -Enzymes and Introduction to Metabolism: Module convener   
• BI629 -Proteins: Structure and Function:  
• BI600 -Research project: Module convenor