Our interests are centered on the application of Nuclear Magnetic Resonance
(NMR) spectroscopy to the study of protein and nucleic acid structures.
Earlier structures included a peptide binding domain (PDZ domain) involved in signal transduction
and a protein homeodomain (PBX) ternary complex with DNA and a small peptide. We also studied the solution
structure of nucleic acid hairpins, and CNP, RICH, GlgS, YbeD, aIF2-beta, CsrA, YbcJ, TcUBP1, GatB, YggX,
ChaB, NECAP1, alpha- & gamma-adaptins and other proteins.
Our principal studies are on the structure and function of the poly(A) binding proteins (PABC, RRM, etc.), the ER
interactome (calnexin, ERp57, PDI, etc.) and apoptotic proteins of the Bcl-2 family (Bcl-w, Bcl-xL, Bak, Mcl-1, tBid, etc.).
We work as well on developing new methodology for measuring residual dipolar couplings
using polymer stabilized liquid crystalline media.
Our laboratory combines techniques from chemistry, molecular biology and bioinformatics in the
quest for a deeper understanding of molecular recognition in biological systems.
BAK dimer, Moldoveanu et al. (2006), Mol. Cell, 24(5):677-688