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Research interests

The relationship between the structure of a protein and its function is vital to understanding how molecules give rise to biological effects. However, there is an emerging realisation that it is the flexibility and dynamics of proteins that in many cases drives their functional activity. Understanding this relationship is the next step in our understanding of basic life processes.

The scientific approach we take is to apply a broad range of high-level biophysical techniques, giving detailed quantitative information that provides novel insight. The lab has three major research strands:

New biotechnology

We are developing new experimental approaches to rapidly test proteins for their native function, based on accurate detection of their dynamics and flexibility, what we term the 'dynamic profile'. This technology has major industrial applications but also potential for use in a clinical setting.

Enzyme dynamics

One of the big questions in enzymology is the role of the motion of the protein, the enzyme dynamics. In particular, what is the role of dynamics in determining enzyme specificity, mechanism and activity. These are challenging questions, but answering them will contribute to enzyme biotechnology, for example improving enzyme (re)design.

Disordered protein biophysics

There is a very deep rooted notion that proteins must adopt very fixed structures and this fixed structure defines the functional abilities of the protein. However, a very high percentage of proteins contain large regions that are structurally disordered, lacking a defined structure as we currently define it. We are probing the functional role of structural disorder and how this feeds into molecular signalling networks.

Willing to supervise PhD

We have projects available in biopharmaceutical technology and biocatalysis.

Keywords

  • Enzyme
  • Catalysis
  • Fluorescence Spectroscopy
  • Biophysics
  • Single molecule
  • Biotechnology

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Isotopes Chemical Compounds
Enzymes Chemical Compounds
Kinetics Chemical Compounds
Flavin Mononucleotide Chemical Compounds
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Hydrogen Chemical Compounds
Catalysis Medicine & Life Sciences
NAD Chemical Compounds

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Projects 2014 2019

MRC P2D - Driving Industrial Adoption of QUBES

Pudney, C.

1/08/1831/07/19

Project: Research council

Monitoring Amyloid Beta Aggregation in Cellulo

Pudney, C.

1/11/1731/10/18

Project: Research council

Redefining Protein Engineering for Biocatalysis

Pudney, C.

1/03/1731/10/17

Project: Research council

Delivering the Impact of QUBES througha Biotech

Pudney, C.

28/10/1631/03/17

Project: Research council

GCRF - Safe Drugs for Developing Countries

Pudney, C.

18/07/1617/03/17

Project: Research council

Research Output 2006 2019

Excitation-energy-dependent molecular beacon detects early stage neurotoxic aβ aggregates in the presence of cortical neurons

Gulácsy, C. E., Meade, R., Catici, D. A. M., Soeller, C., Pantos, G. D., Jones, D. D., Alibhai, D., Jepson, M., Valev, V. K., Mason, J. M., Williams, R. J. & Pudney, C. R., 20 Mar 2019, In : ACS Chemical Neuroscience. 10, 3, p. 1240-1250 11 p.

Research output: Contribution to journalArticle

Open Access
File
1 Citation (Scopus)

Uncovering the relationship between the change in heat capacity for enzyme catalysis and vibrational frequency through isotope effect studies

Jones, H. B. L., Crean, R. M., Matthews, C., Troya, A. B., Danson, M. J., Bull, S. D., Arcus, V. L., Van Der Kamp, M. W. & Pudney, C. R., 1 Jun 2018, In : ACS Catalysis. 8, 6, p. 5340-5349 10 p.

Research output: Contribution to journalArticle

Open Access
File
Vibrational spectra
Isotopes
Catalysis
Specific heat
Substitution reactions
5 Citations (Scopus)

A complete thermodynamic analysis of enzyme turnover links the free energy landscape to enzyme catalysis

Jones, H. B. L., Wells, S. A., Prentice, E. J., Kwok, A., Liang, L. L., Arcus, V. L. & Pudney, C. R., Sep 2017, In : FEBS Journal. 284, 17, p. 2829-2842

Research output: Contribution to journalArticle

Catalysis
Thermodynamics
Enzymes
Hot Temperature
Viscosity
8 Citations (Scopus)

Steady-State Kinetics of α-Synuclein Ferrireductase Activity Identifies the Catalytically Competent Species

McDowall, J. S., Ntai, I., Hake, J., Whitley, P. R., Mason, J. M., Pudney, C. R. & Brown, D. R., 4 May 2017, In : Biochemistry. 56, 19, p. 2497–2505 9 p.

Research output: Contribution to journalArticle

Open Access
File
alpha-Synuclein
Kinetics
Neurodegenerative diseases
Enzyme activity
Neurodegenerative Diseases