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From protein dynamics to protein function and stability using NMR spectroscopy and computer simulation:

Proteins are flexible molecules that often undergo conformational changes to perform biological functions. For this reason, knowledge of the internal dynamics of proteins is crucial to an understanding of the details of their functions and mechanisms of action.

The focus of my laboratory is to understand the relationship between the structure, stability, and dynamics of proteins. In particular we investigate how the structure and dynamics of a protein affect molecular recognition, binding specificity, allostery and stability. To this end, we take a multi-disciplinary approach combining the strengths of biophysical, biochemical and in vivo techniques, with particular emphasis on solution NMR spectroscopic and computational methods.

Specific targets of our research program:

We are currently working on elucidating how two families of RNA-binding proteins, TTP and C. elegans tandem zinc finger proteins, regulate their mRNA targets and on characterizing the allosteric mechanism of Scapharca dimeric hemoglobin.