Welcome to the ARG
The research group of Professor Niels H. Andersen is located at the University of Washington. Professor Andersen is a faculty member of the Department of Chemistry and the Biomolecular Structure and Design Program.
The Group is perhaps best known for the TrpCage miniprotein. The 20-residue protein, containing secondary and tertiary structural elements and an aromatic/hydrophobic core, is an excellent target for computer simulations; an all-atom structure prediction was published by Simmerling and Roitberg shortly after the structure was presented (PDB 1L2Y).
Secondary Structure and Chemical Shift
Secondary structure elements, modeled in peptide systems, remain a strong area of interest for the Group. Our studies have focused on helical, hairpin, and sheet systems. Our preferred source for analytical data is NMR or, more specifically, the chemical shift deviations (CSDs) that arise from peptides adopting a folded conformation. CSD observations are supplemented by nOe analysis and circular-dichroism spectroscopy data. Proton chemical shifts are currently the best understood. The Group has recently released CSDb2, the second version of its in-house application for the analysis of proton CSDs.
While proton CSDs remain a strong area of interest, the Group is increasingly employing the 13C chemical shifts of backbone carbonyls as an additional measure of fold; one that correlates well with FT-IR studies.