Residual Dipolar Couplings: Measurements and Applications to Biomolecular Studies

Since the first successful demonstration of the tunable alignment of ubiquitin in an anisotropic liquid crystal medium only eight years ago, much progress has been made in both NMR pulse techniques for the measurements of various residual dipolar couplings (RDCs) in both proteins and nucleic acids, and applications of RDCs to many important problems in biochemistry and structural biology. In this annual report, we first review recent developments in NMR techniques for the measurements of many types of RDCs in both proteins and nucleic acids, especially a series of novel techniques for improving spectral resolution, signal to noise ratio and saving experimental time. We then describe the applications of RDCs to proteins including automated resonance assignment, structure determination, ligand-protein and proteinprotein dockings as well as protein folding. ∗Immunology Division, BRI, City of Hope, Duarte Rd. 1500, Duarte, CA 91010, USA. †Dartmouth Computer Science Department, Hanover, NH 03755, USA. ‡Dartmouth Chemistry Department, Hanover, NH 03755, USA. §Corresponding authors: Weidong Hu, Immunology Division, BRI, City of Hope, Duarte Rd. 1500, Duarte, CA 91010, USA. Email: [email protected] and Lincong Wang, 6211 Sudikoff Laboratory, Dartmouth Computer Science Department, Hanover, NH 03755, USA. Email: [email protected]. Weidong Hu and Lincong Wang contribute equally to the work.