Department 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, including research into the analysis of NMR data using Deep Learning 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 or apply here
Overarching a BIIIIIIG magnet
Hansen et al. (2011)
Double-quantum arginine 15Nh experiment brings the terminal amines into focus
Mackenzie et al. J. Biomol NMR. (2017)
FID-Net: A Versatile Deep Neural Network Architecture for NMR Spectral Reconstruction and Virtual Decoupling
Karunanithy and Hansen. J. Biomol NMR. (2021)
Virtual Homonuclear Decoupling in Direct Detection NMR Experiments using Deep Neural Networks
Karunanithy et al. chemRxiv (2021)
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)
A Distal Regulatory Region of a Class I Human Histone Deacetylase
Werbeck, Shukla et. al. Nature Comm. (2020)
Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange
Karunanithy et. al. J. Phys. Chem. Lett. (2020)
Thanks for recent financial support from:
