Research Projects
A. Dynamical studies of functionally altered mutants of the tryptophan repressor protein
This project involves the NMR dynamical studies of functionally altered variants of the tryptophan repressor protein, a member of a large family of proteins that regulate the expression of metabolic genes by binding to DNA operator regions (see Figure). This research is in collaboration with Dr. Jannette Carey, Professor of Biochemistry at Princeton University. Our interest centers on understanding the role(s) played by molecular flexibity (i.e. internal motions of atoms) to modulate the functional properties of the protein. Functional residues of proteins are often located on solvent accessible surface loops positioned within a more stable protein core. The biological activity of a protein is thus intrinsically linked to molecular flexibility. The issues of dynamics and molecular flexibility have been particularly important when trying to understand the fundamental principles underlying molecular recognition, protein-protein and protein-nucleic acid interactions. To this effect, our research focuses on the issue of molecular recognition by bacterial DNA-binding proteins, and in particular, on understanding the dynamical properties of a temperature-sensitive mutant of the tryptophan repressor protein (L75F-TrpR) whose biological and biophysical properties cannot be simply explained by small structural changes when compared to the wild-type repressor protein (WT-TrpR).
Publications
Robert Tyler, Istvan Pelczer, Jannette Carey, and Valerié Copié, "Three-dimensional solution structure of apo-L75F, a temperature-sensitive mutant of the tryptophan repressor protein ." Biochemistry, Vol. 41, pp. 11954-11962 (2002)
Personnel:
Valérie Copié
Keywords:
Biophysical, NMR, Protein Chemistry, Spectroscopy, Structure
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