Protein structure. molecular motors. protein engineering. macromolecular assembly. muscle contraction
The focus of our research is the study of
macromolecular structure and assembly with our efforts concentrated on the
analysis of the protein myosin and its interaction with actin. Actin and
myosin are highly conserved proteins that participate in determination of
cell shape. cellular motility. cytokinesis and contractility. Our research
uses the techniques of protein biochemistry. molecular genetics. immunochemistry. electron microscopy and crystallography to analyze myosin
structure. assembly and function. These studies have contributed to the
current understanding of myosin structure and have culminated in the
determination of the structure of the myosin motor domain at 2.8 Å
resolution. The molecular model of myosin is revealing exciting new
insights into the fundamental mechanism of biological energy
transformation. These structural studies are complemented by the use of
molecular genetics and site directed mutagenesis of cloned myosin genes.
In addition to its role in generating force and motion in all eukaryotic
cells. myosin is a major structural component of the contractile organelle
of muscle and non-muscle cells. We are investigating this role by
expression of GFP-myosin chimeras and fluorescent microscopy of living
cardiac and skeletal muscle cells.
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