Display Accessibility Tools

Accessibility Tools

Grayscale

Highlight Links

Change Contrast

Increase Text Size

Increase Letter Spacing

Readability Bar

Dyslexia Friendly Font

Increase Cursor Size

MICHIGAN STATE UNIVERSITY
College of Natural Science
Department of Chemistry

David P. Weliky

Photo of David P. Weliky

Research

Biophysical Chemistry and Nuclear Magnetic Resonance

(Research Description PDF)

Structures of the influenza virus HA2 fusion peptide in membrane deduced from our NMR data.
Structures of the influenza virus HA2 fusion peptide in membrane deduced from our NMR data.

We are a biophysical chemistry group that is focused on understanding the mechanism of entry by viruses enveloped by a membrane. Many important human pathogens are enveloped viruses, including Human Immunodeficiency (HIV), Influenza, Measles, Rabies, West Nile, Zika, Ebola, SARS, and MERS. Each virus has evolved a protein in its membrane that catalyzes the joining (“fusion”) of the virus membrane with the membrane of the target cell. We are studying the glycoprotein 41 kDa (gp41) fusion protein of HIV and hemagglutinin subunit 2 (HA2) fusion protein of influenza. Our work and contributions include the protein structures and locations in membrane. We also study the changes in membrane structure associated with the protein. A significant fraction of our effort is in development and application of “solid-state”, i.e. anisotropic nuclear magnetic resonance (NMR) to these proteins. We also apply a variety of other biophysical methods including circular dichroism spectroscopy, fluorescence spectroscopy, hydrogen-deuterium exchange mass spectrometry, X-ray crystallography, and electron microscopy. We also have a significant effort in protein synthesis and chromatographic purification that includes molecular biology and protein expression in bacteria, solid-phase peptide synthesis, and native chemical ligation. A side-project in the laboratory is NMR analysis of expressed proteins in bacterial inclusion bodies, which are commonly-formed solid protein aggregates. We want to understand why these aggregates form, and the degree of folding of individual proteins within the aggregates. Our NMR methodology focuses on quantitative determination of distributions of populations of protein structures and membrane locations, with a particular emphasis on the rotationalecho double-resonance (REDOR) approach which is robust and amenable to quantitative analysis.

Models for influenza HA2-mediated membrane apposition based on our experimental data.
Models for influenza HA2-mediated membrane apposition based on our experimental data.