Welcome to the Molecular Biophysics
and Engineering Lab at Ole Miss!
Molecular Biophysics is a rapidly evolving interdisciplinary area of research at the interface of biology, chemistry, physics, and engineering. We seek to understand the mechanics of biology from the single molecule to complex system levels, such as how different parts of a cell move and function. We are specifically looking at the cell’s cytoskeletal machinery. Using novel approaches to better understand life at the molecular level will be pivotal in discovering the mechanisms of disease and thus developing more targeted therapeutics.
The lab is currently investigating ensemble interactions of motor proteins, crosslinkers, and their associated filaments to understand how molecular-level interactions result in large-scale cellular tasks, such as division, motility, and muscle contraction. We evaluate these properties using biophysical techniques such as optical trapping, fluorescence microscopy, and QCM-D.
Our research can be divided into three main areas:
Motor Protein Biophysics
Using high resolution optical trapping and fluorescence microscopy, we can evaluate the single molecule properties of motor proteins. This includes their motility and force generation capabilities, which can be measured on the nanometer and piconewton levels, respectively.
Synergy of Engineered Cytoskeletal Assemblies
Traditional motor protein experiments involve a single molecule interacting with or moving along a single substrate. While this yields important information that cannot be attained from bulk experiments, the assay conditions do not accurately represent physiological conditions. The cell environment has structures of various hierarchies, from filament bundles to the dynamic mitotic spindle assembly. Therefore, reconstituting and probing systems at higher levels of complexity in vitro would yield more physiologically relevant data and reveal ensemble mechanistic information that describes how the cytoskeleton works together to perform large-scale cellular tasks.
Physical Properties of Cytoskeletal Building Blocks
Individual components or domains of proteins have specific sequences that are essential for their function. Modulating even a single amino acid side group can alter the affinity of a protein for its substrate. Investigating the biophysical chemistry of motor protein/cytoskeletal filament interactions using spectroscopic methods can reveal the foundational principles of how these systems function.