|
About Us
|
|
Research in the Mosberg lab focuses on structural studies of membrane proteins, especially G-protein-coupled receptors, and on the structure-based design of biologically active compounds with high specificity and activity toward these membrane receptors (e.g. opioid, orphanin, protease-activated and melanocortin receptors). More generally, we are interested in using experimentally obtained or modeled protein structures to design small molecule receptor ligands or small molecule inhibitors of protein-protein interactions. The experimental approaches used include solution and solid-phase synthesis of peptides and organic compounds, their analysis by HPLC, LCMS, CD and various NMR-techniques and protein engineering by mutagenesis to probe protein structure and protein-ligand interactions. The theoretical methods employed include conformational analysis of peptide ligands and protein fragments (conformational search/molecular mechanics) and the use of existing and the development of new bioinformatics tools for protein structure prediction (homology modeling, fold recognition and ab-initio modeling software/servers), particularly directed to modeling of membrane proteins.
For more information on specific current and recent projects, please browse our web site!
|
External Funding
|
|
DA 03910, H. I. Mosberg, PI
NIH/NIDA
Conformation-Selectivity Relations of Opioid Peptides
|
|
P50 DA 00254 J. H. Woods, PI
NIH/NIDA
Narcotic Drug and Opiate Peptide Basic Research Project
|
|
R01 HL 46417, R. R. Neubig, PI
NIH
Structural basis of Receptor/G protein function
|
|
A. Hasan, PI
Michigan Life Sciences Corridor Fund
Thrombostatin. A Novel Anti-Platelet Agent
|
|
R21 GM61299, A. L. Lomize, PI
NIH/NIGM
Thermodynamic model of transmembrane alpha-bundles
|
|
R42 HL61981 A. Hasan, PI
NIH/NHLBI&Thromgen, Inc.
Thrombostatin in the Folts Model for Coronary Thrombosis
|
|
|
