Department of Chemistry & Biochemistry

Nuclear Magnetic Resonance

The NMR lab hosts two magnets located in 121D Dobo Hall. The 300 MHz and 600 MHz NMR spectrometers are available to all researchers and students at UNCW. Access of the instrumentation in the NMR facility is obtained via training by the facility director, Dr. Shu-Yu Liao. Training guides for new users can be found in the Documentation.The NMR facility currently does not service external users (i.e. local companies). The primary users of the NMR lab are from the Chemistry and Biochemistry Department but CheIF welcomes researchers from different colleges.

Please contact Dr. Shu-Yu Liao, liaos@uncw.edu for information.

Research Interest of Dr. Shu-Yu Liao

The structure of proteins is essential to understand detailed mechanisms of how proteins work. Despite the large amount of protein structures deposited in the protein data bank (PDB), only a small fraction of those are membrane proteins. Their intrinsic hydrophobicity makes purification and structure determination of membrane proteins extremely challenging. Solid-State Nuclear Magnetic Resonance (SSNMR) spectroscopy is a rapid developing indispensable technique to elucidate the structure and dynamics of membrane proteins. Unlike solution NMR and X-ray crystallography, SSNMR can study membrane proteins in their native environment, without the use of detergents that might perturb the protein structure and function.

Using SSNMR to determine the extracellular domain of a membrane protein increases the proton conduction activity

M2conduction

Using SSNMR to investigate the drug binding in different length of the same membrane protein by looking at chemical shift perturbation

drugbinding

Publications

8. MD Gelenter, T Wang, S Liao, H O’Neill, M Hong, “2H-13C Correlation Solid-State NMR for Investigating Dynamics and Water Accessibilities of Proteins and Carbohydrates”, J. Biomol. NMR 68, 257-270 (2017)

7. V Mandala, SY Liao, BS Kwon, M Hong, “Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy”, J. Mol. Biol. 429, 2192-2210 (2017)

6. H Yao, M Lee, SY Liao, M Hong, "Solid-State NMR Investigation of the Structural Topology and Lipid Interactions of a Viral Fusion Protein Chimera Containing the Fusion Peptide and Transmembrane Domain”, Biochemistry 55, 6787-6800 (2016)

5. SY Liao, M Lee, T Wang, Sergeyer V, M Hong, "Efficient Dynamic Nuclear Polarization NMR of Membrane Proteins: Optimal Sample Preparation Protocols, Sensitivity, and Radical Location", J. Biomol. NMR 64, 223-237 (2016)

4. BS Kwon, D Tietze, PB White, SY Liao, M Hong, "Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain", Protein Sci. 24, 1087-1099 (2015)

3. SY Liao, Y Yang, D Tietze, M Hong, "The Influenza M2 Cytoplasmic Tail Changes the Proton-Exchange Equilibria and the Backbone Conformation of the Transmembrane Histidine Residue to Facilitate Proton Conduction", J. Am. Chem. Soc. 137, 6067-6077 (2015)

2. SY Liao, KJ Fritzsching, M Hong, "Conformational analysis of the full-length M2 protein of the Influenza A virus using solid-state NMR", Protein Sci. 22, 1623-1638 (2013)

1. K Schmidt-Rohr, KJ Fritzsching, SY Liao, M Hong, "Spectral Editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination", J. Biomol. NMR 54, 343-353 (2012)