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School of Physical and Chemical Sciences

Dr Arianna Fornili

Arianna

Senior Lecturer | Director of the Artificial Intelligence for Drug Discovery MSc programme

Email: a.fornili@qmul.ac.uk
Telephone: +44 (0)20 7882 8446
Room Number: G. O. Jones Building, Room 219

Profile

Dr Arianna Fornili is a Senior Lecturer in Computational Organic Chemistry and former Intermediate Basic Science Research Fellow of the British Heart Foundation. She joined QMUL after holding postdoctoral research associate positions at the Randall Division of Cell and Molecular Biophysics (King’s College London) and the DIBIT San Raffaele Scientific Institute in Milan. Her research group (https://afornililab.wordpress.com/) focuses on the computational modelling of protein dynamics to understand protein function, elucidate the molecular basis of disease and develop small molecules with therapeutic applications.

Undergraduate Teaching

  • Essential Skills for Chemists (Tutorials) (CHE100)
  • Pharmaceutical Chemistry (CHE206A)

  • Pharmaceutical Chemistry (CHE206B)

  • Introduction to Scientific Programming (SBC5291)

  • Introduction to Scientific Programming (SBC5292)

Postgraduate Teaching

Chair of the examination board for Chemical Research MSc.

Research

Research Interests:

My research activity is focused on the computational study of protein dynamics and its relationship to protein function.

The main interest of the group is the study of structural, dynamical and mechanical properties of proteins from the cardiac muscle. Heart contraction arises from a complex interplay of precisely timed molecular motions and the identification of new therapeutic targets for cardiomyopathies relies on a deep understanding of these mechanisms. Combining Molecular Modelling, Molecular Dynamics simulation and Bioinformatics techniques, we investigate how post-translational modifications and cardiomyopathy-related mutations affect the protein motion and stability.

The group is also involved in the development of computational methods for the study of conformational transitions in proteins. In addition to promoting the motion of molecular motors, conformational changes can be essential for many protein functions and they are often required for protein-protein interaction and allosteric regulation. The group aims at improving both the sampling and the detection of biologically relevant conformational transitions, which are usually beyond the timescale of traditional molecular simulations.

Research Department

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