Institute of Structural and Molecular Biology
Division of Biosciences
University College London
Darwin Building - Gower Street
WC1E 6BT London, UK
The Hansen Lab focuses on the study of protein dynamics using nuclear magnetic resonance (NMR) techniques. NMR method development is a major part of our research, as well as the combination of NMR with computational tools. We are particularly interested in the dynamics, function, and regulations of human histone deacetylases (HDACs) and domains of the von Willebrand Factor (vWF).
We currently have availability for a postdoctoral fellow researching protein dynamics and/or NMR spectroscopy. If you are interested, then please send an email to d.hansen[at]ucl.ac.uk with your CV and motivation
Overarching a BIIIIIIG magnet
Hansen et al. (2011)
HDAC8 loop dynamics
Kunze et al. JACS (2013)
Structure of the Von Willebrand Factor on the front of Blood.
Shiltagh et al. Blood (2014)
Theoretical calculation of relaxation rates in AX4 spin systems
Werbeck et al. J. Magn. Reson (2014)
Characterising active site conformational heterogeneity
Zeymer et al. Angewandte Chemie Int. Ed (2016)
Rotational dynamics of arginine side-chains report on the interactions formed
Gerecht et al. Chem Comm. (2017)
Double-quantum arginine 15Nh experiment brings the terminal amines into focus
Mackenzie et al. J. Biomol NMR. (2017)
Measurement of 15N Longitudinal Relaxation Rates in 15NH4+ Spin Systems
Hansen J. Magn. Reson (2017)
Using 13C-direct detection to quantify arginine Side-Chain Hydrogen Exchange
Mackenzie et al. ChemPhysChem (2019)
Using 13C-direct detection to quantify side-chain dynamics in large proteins
Pritchard et al. Nature Comm. (2019)
Determining isoleucine side-chain rotamer-sampling in proteins from 13C chemical shift.
Siemons et. al. Chem Comm. (2019)
Thanks for recent financial support from:
