David Weliky
Professor Office: 41 Chemistry
Phone: 517-355-9715 281 /
Websites: Research Group - Area
Awards & Honors
Genealogy/Graduates
Nuclear Magnetic Resonance of Biological and Inorganic Systems
(Research Description PDF - 1208 kb)Solid state nuclear magnetic resonance spectroscopy is a powerful approach to determine atomic-resolution structure and dynamics in solid systems. Our research currently focuses on applications of solid state NMR to problems in membrane fusion and inorganic materials.
Membrane Fusion. Fusion between cells and cellular components has an essential role in living organisms and plays an important part in such significant physiological processes as egg fertilization and synaptic transmission in the nervous system. Membrane fusion is also an important step in HIV infection of human cells and is mediated by the hydrophobic "fusion peptide" region of the gp41 viral envelope protein. We are using solid state NMR to determine the conformation, membrane orientation, and oligomerization state of the membrane-bound HIV fusion peptide. These data are being incorporated into an atomic-resolution structural model of fusion-peptide induced membrane fusion. We have a parallel effort in influenza viral fusion which is also catalyzed by a fusion peptide.
NMR of Chalcogenide Materials. Thio-, seleno-, and tellurophosphates and chalcostannates form a diverse set of compounds with interesting optical, photoconductive, and ferroelectric properties. We are using ambient and high (=400 °C) temperature NMR to characterize the reactants, intermediates, and products in the syntheses of these materials.
Solid State NMR of Uniformly Labeled Peptides. We have a long-term interest in solid state NMR of fully 13C, 15N labeled peptides and proteins, analogous to the highly successful solution NMR methodologies for protein structure determination. At this time, solid state NMR methods are being developed both to assign the individual resonances in the NMR spectra of fully labeled proteins and to determine molecular structure from these spectra. We are applying such methods to determine complete atomic-resolution structures of viral fusion peptides and proteins in membranes.
While doing this research, students learn a variety of skills which could include peptide synthesis, protein expression and purification, inorganic synthesis, design and repair of NMR equipment, NMR theory and pulse sequence development, and computer simulation. Our research is benefiting from the enhanced sensitivity and resolution of the new 900 MHz NMR spectrometer at MSU.
Selected Publications
Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of ß Strand Peptide with Membranes and the Proximity of the Ala-14-Gly-16 Region with Lipid Headgroups, W. Qiang, J. Yang, and D. P. Weliky, Biochemistry 2007, 46, 4997.Solid-State NMR Structural Measurements on the Membrane-Associated Influenza Fusion Protein Ectodomain, J. Curtis-Fisk, C. Preston, Z. Zheng, R. M. Worden, and D. P. Weliky, JACS 2007, 129, 11320.
Cs4P2Se10: A New Compound Discovered with the Application of Solid State and High Temperature NMR, M. A. Gave, C. G. Canlas, I. Chung, R. G. Iyer, M. G. Kanatzidis, and D. P. Weliky, J. Solid State Chemistry 2007, 180, 2877.
Improved Resolution and Detection of 31P-Tl J-Couplings at 21 T in 31P Magic Angle Spinning Spectra of Inorganic Compounds Containing Tl/Bi/P/S, M. A. Gave, K. M. Johnson, M. G. Kanatzidis, and D. P. Weliky, Solid State Nuclear Magnetic Resonance 2008, 33, 12.
Solid-State NMR Spectroscopy of HIV Fusion Peptides Associated with Host-Cell-Like Membranes: 2D Correlation Spectra and Distance Measurements Support a Fully Extended Conformation and Models for Specific Antiparallel Strand Registries, W. Qiang, M. L. Bodner, and D. P. Weliky, JACS 2008, 130, 5459.
