We are interested in protein folding and stability in metalloprotein systems. We are therefore applying the time-honored measurements of hyperfine chemical shifts and relaxation parameters, in addition to the more recently applied techniques of two-dimensional NMR to paramagnetic proteins.
Systems currently under investigation include heme proteins, in which
the paramagnetic center is provided by the heme iron. We are also
studying calcium binding proteins, using paramagnetic lanthanides to substitute
for the calcium. The apoproteins and metal-substitions are important
to both of these lines of investigation.