I am a lecturer and a Wellcome Trust/Royal Society Sir Henry Dale fellow in the department of Life Sciences.
I use Nuclear Magnetic Resonance (NMR) methods to investigate complex biological mechanisms, including protein folding and misfolding, and chaperone mediated proteostasis. All of these events proceed via complex pathways that involve transient, short-lived protein species which are often critical for biological function. Solution NMR spectroscopy is the only available biophysical technique that can characterise, in atomic resolution, the structure and kinetics of formation of protein states even if these are lowly-populated (<5%). My research focuses on the development and application of NMR methods and the combination of these approaches with other biophysical techniques (fluorescence-based methods, mass spectrometry and electron microscopy), computational analysis and functional assays in-vitro and in-cells to investigate the structure and dynamics of interconverting systems.
Current positions available
Please check the group's website for any available vacancies. We are always interested in motivated students and postdocs joining our group.
We currently have a postdoctoral position available. Please apply here.
Karamanos TK, Matthews S, 2023, Biomolecular NMR in the AI-assisted structural biology era: Old tricks and new opportunities., Biochim Biophys Acta Proteins Proteom
Karamanos TK, 2023, Chasing long-range evolutionary couplings in the AlphaFold era, Biopolymers, Vol:114, ISSN:0006-3525, Pages:1-8
et al., 2022, A "Steady-State" Relaxation Dispersion Nuclear Magnetic Resonance Experiment for Studies of Chemical Exchange in Degenerate 1H Transitions of Methyl Groups, Journal of Physical Chemistry Letters, Vol:13, ISSN:1948-7185, Pages:11271-11279
Cawood EE, Clore GM, Karamanos TK, 2022, Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone, Angewandte Chemie, Vol:134, ISSN:0044-8249
Cawood EE, Clore GM, Karamanos TK, 2022, Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone, Angewandte Chemie International Edition, Vol:61, ISSN:1433-7851