My research focusses on the use of molecular modelling techniques to understand the structure and function of proteins. In August 2013 I moved to the Structural Immunology Group at UCL where I am developing tools to enable the atomistic modelling of low resolution structures generated from small angle scattering experiments. This work is performed as part of the CCP-SAS project. Whilst the research based in my home laboratory is primarily centred around the proteins (and glycoproteins) of the human immune system, my work in the broader project aims to expand the use of atomistic and coarse grained modelling to interpret X-ray and neutron solution scattering experiments in a wide range of soft condensed matter systems (including colloids and polymers). This position combines basic research, software development and the deployment of simulations on high performance computing (HPC) resources.

In my previous role in the centre for computational science (CCS), also within UCL, I studied the use of molecular dynamics and free energy calculations to gain qualitative insight and quantitative information on mutational effects on enzyme function and drug interactions. In particular my work has concentrated on proteins from two major pathologies, HIV and cancer. In the field of HIV, I have worked on the antiretroviral drug target enzymes HIV-1 protease and reverse transcriptase. In the cancer domain, I have studied the epidermal growth factor receptor (EGFR), inhibition of the tyrosine kinase domain of which is used to treat non-small-cell lung cancer, and Histone deacetylase 8 (HDAC8) which has been suggested as a possible target of neuroblastoma differentiation therapy. I maintain strong interests in these projects and more broadly the use of atomistic models in the context of multiscale models, systems biology and medicine.


A full list of all my publications can be found either on my Google Scholar profile or CV.

Recent Papers

G. K. Hui, D. W. Wright, et al., "The solution structures of native and patient monomeric human IgA1 reveal asymmetric extended structures: implications for function and IgAN disease", Biochemical Journal, 2015, online ahead of print, DOI: 10.1042/BJ20150612

S. Wan, B. Knapp, D. W. Wright, et al., "Rapid, Precise, and Reproducible Prediction of Peptide–MHC Binding Affinities from Molecular Dynamics That Correlate Well with Experiment", Journal of Chemical Theory and Computation, 2015, 11(7), DOI: 10.1021/acs.jctc.5b00179

D. W. Wright and S. J. Perkins, "SCT: a suite of programs for comparing atomistic models with small-angle scattering data", Journal of Applied Crystallography, 2015, 48, DOI:10.1107/S1600576715007062

J. B. Swadling, D. W. Wright, et al., "Structure, Dynamics and Function of the Hammerhead Ribozyme in Bulk Water and at a Clay Mineral Surface From Replica Exchange Molecular Dynamics", Langmuir, 2015, 31 (8), DOI: 10.1021/la503685t

I. P. Deuzing, C. Charpentier, D. W. Wright, et al., "Mutation V111I in HIV-2 reverse transcriptase increases the fitness of the nucleoside analogue resistant K65R and Q151M viruses", Journal of Virology, 2014, 89 (1), DOI: 10.1128/JVI.02259-14

D. W. Wright, B. A. Hall, O. A. Kenway, S. Jha and P. V. Coveney, "Computing Clinically Relevant Binding Free Energies of HIV-1 Protease Inhibitors", Journal of Chemical Theory and Computation, 2014, 10 (3), DOI:10.1021/ct4007037

M. B. A. Kunze, D. W. Wright, N. D. Werbeck, J. Kirkpatrick, P. V. Coveney, and D. F. Hansen, "Loop Interactions and Dynamics Tune the Enzymatic Activity of the Human Histone Deacetylase 8", Journal of the American Chemical Society, 2013, 135 (47), DOI:10.1021/ja408184x

D. W. Wright, I. P. Deuzing, et al., "Polymorphism at Position 400 in the Connection Subdomain of HIV-1 Reverse Transcriptase Affects Sensitivity to NNRTIs and RNaseH Activity", PLoS One, 2013, 8 (10), DOI: 10.1371/journal.pone.0074078

D. W. Wright, S. K. Sadiq, G. De Fabritiis and P. V. Coveney, "Thumbs down for HIV: Domain level rearrangements do occur in the NNRTI bound HIV-1 Reverse Transcriptase", Journal of the American Chemical Society, 2012, 134 (31), DOI:10.1021/ja301565k

S. Wan, D. W. Wright and P.V. Coveney, "Mechanism of Drug Efficacy Within the EGF Receptor Revealed by Microsecond Molecular Dynamics Simulation", Molecular Cancer Therapeutics, 2012, 11, DOI: 10.1158/1535-7163.MCT-12-0644-T


Molecular dynamics simulation of drug resistance in HIV-1 protease and reverse transcriptase


CHAIN VPH VPH-SHARE ViroLab ContraCancrum

In November 2012 I was appointed as an associate fellow of the 2020 Science project.


David W Wright
Structural Immunology Group
University College London
Darwin Building
Gower Street
London, WC1E 6BT

Tel: +44 (0)20 7679 2265

LinkedIn: davewwright
Skype: dave.w.wright