Research projects

CIDNP and NMR studies of proteins: conformations, protein-protein interactions binding and protein folding under physiological conditions

CIDNP and NMR studies of antigenic and immunogenic peptide conformations

CIDNP studies of transient conformations of proteins and peptides

2D-NMR Studies on Proteins

PhotoCIDNP and NMR Peptides and Proteins

We investigate the role of vicinal side chain clustering in peptides in stabilizing preferred conformations, and in controlling biomolecular recognition. Our earlier CIDNP and NMR studies of synthetic polypeptide T cell antigens led to the identification of the vicinal Tyr-Tyr side chain aromatic interaction as a conformation determining factor controlling antigen-receptor interaction.
We recently detected the vicinal Try-Glu-H-bond side chain interaction in small linear peptides and in rigidized cyclic architectures, applying photoCIDNP, 2D-ROESY-NMR, and minimum energy searches of peptide structure.
The possibility of selectively affecting conformation, specificity, general extent of the receptor interaction, as well as metabolization, by manipulating pairwise or higher order vicinal side chain clustering should provide new avenues to the rational design of bioactive peptides.

Back to Structural Biology Home