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UCL Division of Biosciences

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Prof Flemming Hansen

Prof Flemming Hansen

Professor and Chair of NMR Spectroscopy

Structural & Molecular Biology

Div of Biosciences

Joined UCL
1st Oct 2010

Research summary

Macromolecular motions and dynamics have fascinated me since the onset of my scientific career. In particular, I am interested in understanding how the molecular dance of a protein relate to biological function and also how the brief excursions that an enzyme makes from its ground state to minor populated excited states influence molecular function.  My main research areas are : (1) Characterise the dynamics and mechanisms of interactions between histone deacetylases (HDACs) and their substrates (2) Develop new NMR methodology to characterise macromolecular motions, interactions, and dynamics, using HDACs as model systems.

Teaching summary

Protein NMR theory, Enzyme Kinetics (BIOC2004), Experimental Biochemistry (BIOC1007).

Education

Other Postgraduate qualification (including professional), ATQ01 - Successfully completed an institutional provision in teaching in the HE sector |
Kobenhavns Universitet
Doctorate, Doctor of Philosophy | 2005
Kobenhavns Universitet
Other higher degree, Master of Science (by research) | 2003
Kobenhavns Universitet
First Degree, Bachelor of Science (Honours) | 2000

Biography

After completing my PhD in biophysical protein chemistry at the University of Copenhagen (2005) I joined the NMR group of prof. Lewis E. Kay at the University of Toronto for postdoctoral training. The main focus of my postdoctoral research was development of NMR methodology to study protein dynamics and develop methods to characterise thermally excited and low populated states of proteins. These excited states often play important roles in ligand binding, molecular recognition, enzyme catalysis, and protein folding, however, they are ‘invisible’ to most of the traditional tools of structural biology. With our new methods we can now determine excited state structures by NMR relaxation dispersion experiment, so long as their lifetimes are between 0.5 and 10 ms and their population exceeds 0.5%. We applied our new methods to determine the structure and dynamics of protein folding intermediates, etc. 

In October 2010 I joined the ISMB with a BBSRC David Phillips fellowship.


Publications