Visiting Scholar, Phi Beta Kappa (2015-2016); Diversity Award, Council for Chemical Research (2015); ACS Award for Encouraging Disadvantaged Students into Careers in the Chemical Sciences (2014), Diversity Champion Award (GT, 2013), Fellow, American Physical Society (APS, 2011); Fellow, American Chemical Society (ACS, 2010); Fellow, American Association for the Advancement of Science (AAAS, 2004). Outstanding Service Award, ACS Georgia Local Section (2012); Vasser Woolley Faculty Felllow (2011-2013);... (read more)
Chemical Dynamics in Complex Environments. Most of chemistry takes place under heterogeneous conditions involving interactions and motions occurring at multiple length scales. We study the interplay between molecular motions —such as reactions or rearrangements— and changes in their environments. The latter can arise because of external driving conditions —such as shearing— or from collective changes in the system —such as from an overall change in the chemical composition driven by the reactions themselves. We use reduced dimensional models which require the introduction of nostationary friction kernels associated with the solvent response. We also use simulations to reveal the complexity in the dynamics of the system and the time-dependent nonuniform environments.
Dynamics of Structured Particles. Nano- and meso- scale particles self-assemble into macroscopic assemblies with a large dynamic range in their properties. We are interested in understanding how the interactions and structure at the shortest scales leads to these emergent properties in static and temporal regimes. Examples of such materials include nanorods diffusing through static or mobile scattered and the assembly of amorphous suspensions of Janus particles.
Protein Dynamics and Binding. The adaptive steered molecular dynamics (ASMD) allows us to obtain the energetics of a protein along a chosen path quickly and accurately. We are using ASMD to understand the path along which a protein can be opened by revealing which structural components (such as hydrogen bonds) persist along the path. In addition, we have used minimalist lattice and off-lattice models to obtain rich insight characterizing the universal behavior of protein folding and unfolding without suffering high computational costs. Monte Carlo simulations of designed minimalist proteins are being analyzed through novel projections to provide a better understanding of the connection between structure and protein dynamics.