Research Group(s)

• Biorefinery Engineering
• Molecular Systems and Biomaterials

Robin Curtis joined the department in 2003.  He is a member of the Multiscale, Theory and Computation group in CEAS. Previously, he completed his PhD in 2000 at the University of California at Berkeley under the supervision of John Prausnitz and Harvey Blanch.  Afterwards, he held post-doctoral positions at the University of California at Los Angeles and at Rive University in Houston under the supervision of Michael Deem. 

Our research involves understanding the behaviour of various systems from knowledge of the intermolecular interactions. In a lot of cases, the thermodynamic and/or structural properties of systems can be determined from statistical-mechanical models whose inputs are given by a set of two-body interactions. In this work, solvent-averaged two-body interactions are determined using a combination of experiments and atomic-level simulations. 

This type of approach is used for a range of projects. In one project, weak biologically-relevant protein-protein interaction are being measured using a recently developed high throughput light scattering method.  This work is novel in that most methods for characterizing protein interactions are useful only when the proteins form well-lived complexes.  Using our approach we are able to characterize transient complexes which can sample multiple encounter interactions.  This approach is being applied to the study of electron transfer proteins in close collaboration with Andrew Munro (Faculty of Life Sciences, University of Manchester).  In these systems, the interacting proteins have mutiple binding partners so that there is an evolutionary constraint to sample weaker protein-protein interactions.

In another project, we are characterizing the interactions between homopolypeptides, in which case, the secondary structure and the amyloidogenicity of the peptide can be controlled by changing the solvent conditions.  These measurements allow us to understand the role of helicity in protein aggregation and fibril formation.  Our results have revealed some important biological implication of Hofmeister effects, which refer to the effect of changing the nature of the salt type.