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Dr Neil Kad

Senior Lecturer in Molecular Biophysics

Biosciences

 

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.

  1. DNA Repair
  2. Muscle Contraction
  3. 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.

ORCID: 0000-0002-3491-8595


External link to lab homepage

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Also view these in the Kent Academic Repository

Article
Kad, N. and Van Houten, B. (2016). DNA repair: Clamping down on copy errors. Nature [Online]. Available at: http://dx.doi.org/10.1038/nature20475.
Lin, J. et al. (2016). Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing. Nucleic acids research [Online]. Available at: http://dx.doi.org/10.1093/nar/gkw518.
Kong, M. et al. (2016). Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process. Molecular Cell [Online] 64:376-387. Available at: http://doi.org/10.1016/j.molcel.2016.09.005.
Walcott, S. and Kad, N. (2015). Direct Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation. PLoS computational biology [Online] 11. Available at: http://www.dx.doi.org/10.1371/journal.pcbi.1004599.
Kad, N., Cheruvara, H. and Mason, J. (2015). Intracellular Screening of a Peptide Library to Derive a Potent Peptide Inhibitor of α-Synuclein Aggregation. Journal of Biological Chemistry [Online] 290:7426-7435. Available at: http://dx.doi.org/10.1074/jbc.M114.620484.
Simons, M. et al. (2015). Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe. Scientific reports [Online] 5:18486. Available at: http://doi.org/10.1038/srep18486.
Lin, J. et al. (2014). TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres. Nucleic acids research [Online] 42:2493-2504. Available at: http://dx.doi.org/10.1093/nar/gkt1132.
Acerra, N. et al. (2014). Retro-inversal of intracellular selected β-amyloid-interacting peptides: implications for a novel Alzheimer's disease treatment. Biochemistry [Online] 53:2101-2111. Available at: http://dx.doi.org/10.1021/bi5001257.
Acerra, N. et al. (2014). Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomers. Protein science : a publication of the Protein Society [Online] 23:1262-1274. Available at: http://dx.doi.org/10.1002/pro.2509.
Van Houten, B. and Kad, N. (2014). Investigation of bacterial nucleotide excision repair using single-molecule techniques. DNA repair [Online] 20:41-48. Available at: http://dx.doi.org/10.1016/j.dnarep.2013.10.012.
Kad, N. and Van Houten, B. (2014). Single molecule approaches: watching DNA repair one molecule at a time: Preface. DNA repair [Online] 20:1. Available at: http://dx.doi.org/10.1016/j.dnarep.2014.06.007.
Desai, R., Geeves, M. and Kad, N. (2014). Using Fluorescent Myosin to Directly Visualize Cooperative Activation of Thin Filaments. Journal of Biological Chemistry [Online]:jbc.M114.609743-jbc.M114.609743. Available at: http://dx.doi.org/10.1074/jbc.M114.609743.
Hughes, C. et al. (2014). Single molecule techniques in DNA repair:a primer. DNA repair [Online] 20:2-13. Available at: http://dx.doi.org/10.1016/j.dnarep.2014.02.003.
Acerra, N., Kad, N. and Mason, J. (2013). Combining intracellular selection with protein-fragment complementation to derive Aβ interacting peptides. Protein engineering, design & selection : PEDS [Online] 26:463-470. Available at: http://dx.doi.org/10.1093/protein/gzt021.
Hughes, C. et al. (2013). Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes. Nucleic acids research [Online] 41:4901-4912. Available at: http://dx.doi.org/10.1093/nar/gkt177.
Zhang, C. et al. (2012). A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate. Biophysical journal [Online] 103:728-737. Available at: http://dx.doi.org/10.1016/j.bpj.2012.07.033.
Dunn, A. et al. (2011). Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA. Nucleic acids research [Online] 39:7487-7498. Available at: http://dx.doi.org/10.1093/nar/gkr459.
Kad, N. et al. (2010). Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins. Molecular cell [Online] 37:702-713. Available at: http://dx.doi.org/10.1016/j.molcel.2010.02.003.
Kad, N., Trybus, K. and Warshaw, D. (2008). Load and Pi control flux through the branched kinetic cycle of myosin V. The Journal of biological chemistry [Online] 283:17477-84. Available at: http://dx.doi.org/10.1074/jbc.M800539200.
Book section
Wang, J. et al. (2017). Integrating Optical Tweezers, DNA Tightropes, and Single-Molecule Fluorescence Imaging: Pitfalls and Traps. in: Single-Molecule Enzymology: Nanomechanical Manipulation and Hybrid Methods. Elsevier, pp. 171-192. Available at: https://doi.org/10.1016/bs.mie.2016.08.003.
Springall, L., Inchingolo, A. and Kad, N. (2016). DNA-Protein Interactions Studied Directly Using Single Molecule Fluorescence Imaging of Quantum Dot Tagged Proteins Moving on DNA Tightropes. in: Leake, M. C. ed. Chromosome Architecture. Springer, pp. 141-150. Available at: http://www.dx.doi.org/10.1007/978-1-4939-3631-1_11.
Kad, N. and Van Houten, B. (2012). Dynamics of lesion processing by bacterial nucleotide excision repair proteins. in: Progress in Molecular Biology and Translational Science. Elsevier, pp. 1-24.
Showing 22 of 32 total publications in KAR. [See all in KAR]
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My key research areas are:

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

image

fig 1

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
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Enquiries: Phone: +44 (0)1227 823743

School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ

Last Updated: 18/05/2017