Welcome!

We currently have a postdoctoral position available, if you are interested in applying/developing methods to study dynamic chaperone complexes email T.Karamanos@imperial.ac.uk

September 2020

September 2020

Karamanos et al., PNAS 2019

Karamanos et al., PNAS 2019

Novel insights into Hsp40-mediated regulation of the chaperone network

Karamanos et al., PNAS 2020

Karamanos et al., PNAS 2020

An S/T motif controls reversible oligomerization of the Hps40 chaperone DNAJB6b

Cawood et al., JACS 2020

Cawood et al., JACS 2020

Covalent ligands modulate amyloid assembly pathways

Karamanos et al., JBNMR 2020

Karamanos et al., JBNMR 2020

Conformations of methyl side-chains using RDC data

Karamanos et al., eLife 2019

Oligomers on pathway to amyloid

Karamanos et al., JACS 2016

Karamanos et al., JACS 2016

Real-time NMR on a protein folding intermediate with NUS

Karamanos et al., Mol. Cell, 2014

Visualization of transient interactions in the early stages of amyloid assembly

September 2020

September 2020

Karamanos et al., PNAS 2019

Karamanos et al., PNAS 2019

Novel insights into Hsp40-mediated regulation of the chaperone network

Karamanos et al., PNAS 2020

Karamanos et al., PNAS 2020

An S/T motif controls reversible oligomerization of the Hps40 chaperone DNAJB6b

Cawood et al., JACS 2020

Cawood et al., JACS 2020

Covalent ligands modulate amyloid assembly pathways

Karamanos et al., JBNMR 2020

Karamanos et al., JBNMR 2020

Conformations of methyl side-chains using RDC data

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Research Mission

We use Nuclear Magnetic Resonance (NMR) methods to investigate complex biological mechanisms, including protein folding and misfolding, and chaperone mediated proteostasis. By combining NMR with fluorescence-based techniques, mass spectrometry and electron microscopy we aim to develop new approaches that visualize these events across the microscopic to the macroscopic scales.

Contact Us

Department of Life Sciences, Imperial College London

T.Karamanos@imperial.ac.uk