Molecular Biophysics and Engineering Lab

The University of Mississippi

Welcome to the Molecular Biophysics

and Engineering Lab at Ole Miss!

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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 focusing on how single molecule characteristics of proteins called “molecular motors” affect their surrounding cytoskeletal environment and overall cell function.  We evaluate these properties using biophysical techniques such as optical trapping and fluorescence microscopy.

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.

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.