Frank P. Shewmaker, Ph.D., Assistant Professor
B.S., Biochemistry, Auburn University
Ph.D., Biochemistry, Tulane University
Post-Doctoral Training, National Institutes of Health
4301 Jones Bridge Road, C2125
Bethesda MD 20814
Phone: (301) 295-3527
Email: fshewmaker@usuhs.mil
Protein Amyloid
Amyloid is a highly-ordered filamentous protein aggregate that is notorious for its association with terrible human disorders such as Parkinson's and Alzheimer's diseases. The formation of amyloid is generally regarded as a misfolding event in which proteins that are normally soluble accumulate into fibrous structures. The determinants of amyloid formation and toxicity are largely unknown, and determining the atomic-level structure of amyloid is challenging because it is not amenable to the conventional structural techniques of x-ray crystallography and solution NMR. Much of the focus of our laboratory is on fundamental issues concerning amyloid formation, structure and toxicity.
Prions
Prions (infectious proteins) of the yeast Saccharomyces cerevisiae represent a special case of amyloid. While most amyloids are not considered infectious, many yeast prions are based on a self-propagating amyloid that is passed between cells during mating or from mother to daughter cells during replication. Because yeast prions are not infectious to people, they offer an easy and safe way to study the fundamentals of amyloid propagation and transmission. Also, the yeast prions are an excellent example of an epigenetic phenomenon; in this case, heritable information is structurally encoded in cytoplasmic proteins instead of within the sequence of DNA. Our laboratory is pursuing issues of prion structure, initiation and propagation.
Frank Shewmaker's list of publications
Electron micrographs of various amyloids:
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Uniformed Services University of the Health Sciences
Department of Pharmacology
4301 Jones Bridge Road
Bethesda, MD 20814
Tel 301-295-3223
FAX 301-295-3220