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Personal profile

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

Fingerprint Dive into the research topics where Christopher Pudney is active. These topic labels come from the works of this person. Together they form a unique fingerprint.

  • 1 Similar Profiles
Isotopes Chemical Compounds
Enzymes Chemical Compounds
Kinetics Chemical Compounds
Flavin Mononucleotide Chemical Compounds
NADPH-Ferrihemoprotein Reductase Chemical Compounds
Hydrogen Chemical Compounds
Catalysis Medicine & Life Sciences
NAD Chemical Compounds

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Projects 2014 2019

Research Output 2006 2019

Synthetic Cannabinoid Receptor Agonists Detection using Fluorescence Spectral Fingerprinting

May, B., Naqi, H., Tipping, M., Scott, J., Husbands, S., Blagbrough, I. & Pudney, C., 15 Oct 2019, In : Analytical Chemistry. 91, 20, p. 12971-12979 9 p.

Research output: Contribution to journalArticle

Open Access
1 Citation (Scopus)

Modelling flavoenzymatic charge transfer events: development of catalytic indole deuteration strategies

Murray, A. T., Challinor, J. D., Gulácsy, C. E., Lujan, C., Hatcher, L. E., Pudney, C. R., Raithby, P. R., John, M. P. & Carbery, D. R., 21 Apr 2016, In : Organic and Biomolecular Chemistry. 14, 15, p. 3787-3792

Research output: Contribution to journalArticle

indoles
Charge transfer
charge transfer
structural analysis
Structural analysis
55 Citations (Scopus)
143 Downloads (Pure)

On the temperature dependence of enzyme-catalyzed rates

Arcus, V. L., Prentice, E. J., Hobbs, J. K., Mulholland, A. J., van der Kamp, M. W., Pudney, C. R., Parker, E. J. & Schipper, L. A., 29 Mar 2016, In : Biochemistry. 55, 12, p. 1681-1688

Research output: Contribution to journalArticle

Open Access
File
Temperature
Enzymes
Catalysis
Protein Stability
Biological systems
8 Citations (Scopus)
113 Downloads (Pure)

The red edge excitation shift phenomenon can be used to unmask protein structural ensembles: implications for NEMO-ubiquitin interactions

Catici, D. A. M., Amos, H. E., Yang, Y., van den Elsen, J. M. H. & Pudney, C. R., 20 Jun 2016, In : FEBS Journal. 283, 12, p. 2272-2284

Research output: Contribution to journalArticle

Open Access
File
Ubiquitin
Polyubiquitin
Ligands
Biophysics
Spectrum Analysis
9 Citations (Scopus)

Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions

Arcus, V. L. & Pudney, C. R., 4 Aug 2015, In : FEBS Letters. 589, 17, p. 2200-2206 7 p.

Research output: Contribution to journalArticle

Specific heat
Hot Temperature
Isotopes
Temperature
Enzymes

Thesis

A Biophysical Approach to Understanding the Temperature-dependence of Enzyme Catalysis

Author: Jones, H., 2019

Supervisor: Leak, D. (Supervisor) & Pudney, C. (Supervisor)

Student thesis: Doctoral ThesisPhD

File

Biophysical factors governing the structure, function, and dynamics of the NF-κB essential modulator protein (NEMO)

Author: Catici, A. M. D., 19 Jun 2019

Supervisor: Leak, D. (Supervisor) & Pudney, C. (Supervisor)

Student thesis: Doctoral ThesisPhD

Exploring the substrate specificity of the antimicrobial peptide transporter BceAB of Bacillus subtilis

Author: Kobras, C. M., 29 May 2019

Supervisor: Pudney, C. (Supervisor) & Gebhard, S. (Supervisor)

Student thesis: Doctoral ThesisPhD

File

Photochemical and Spectroscopic Studies of Ketoaziridines

Author: Gulácsy, C., 8 Jun 2016

Supervisor: Carbery, D. (Supervisor) & Pudney, C. (Supervisor)

Student thesis: Doctoral ThesisPhD

File