What makes Biophysics a powerful apporach is the constant evolution an re-evaluation of the theoretical concepts we use. Below are some of the key theoretical concepts we use in our research, that underpin the research questions that we ask.

Protein structural disorder and dynamics

Proteins are inherenetely flexible molcules. All proteins undergo motion on a range of timescales and there are developing tools and theoretical approaches to detect and interpret this motion. The question is, what is the role of protein flexibility inprotein function?


We are particularlty interest in proteins that lack a fixed structure, comprising regions that are sturcturally disordered. The thermodynamic consequences of structural disorder open up novel mechanistic routes for protein-ligand interactions and provide a new lens though which we can interpret bio-molecular interactions.





Free energy landscape

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Enzyme catalysis

Enzymes are proteins that catalyse chemical reactions. Understanding what the role of the protein is in driving catalysis is a complex question that cannt be simply answered. 


Broadley Enzymes are thought to provide an 'ideal' environment for a chemical reaction to proceed, with the optimisation of electrostatic, steric and dynamic features of the chemical reaction coordinate.


There is an interesting debate regarding the role of protein dynamics in promoting enzyme catalysed reactions, with the potential for vibrational modes of the enzyme or substrate significantley enhancing the enzyme turnover.


Monitoring how a process changes with respect to time gives the kinetics of that process, the rate of change. The kinetics of bio-molecular interactions and reactions provide a wealth of information that can be interpreted to learn fundamental details about the interactions and reactions.


A good example comes from a simple reaction scheme.