Science / Technology - Colloquium
Wednesday, March 25, 2009
4:00 PM-5:00 PM
Olin Hall
107
Hydration shells of normal proteins display both structured and bulk-like
waters. Isomers with considerable bulk-like hydration tend to aggregate.
Our data show that different morphological states of aggregated isomers
differ by hydration distribution profiles and water magnetic resonance
(MR) signals. The results help explain the MR contrast patterns of the
amyloids, a subject of long controversy, and suggest a new approach for
identifying unusual protein aggregation related to disease. As an example,
I will present water proton MR spectroscopic data, thioflavin T
fluorescence, gel electrophoresis and cell toxicity measurements revealing
the relationship between amyloid conformation and amyloid-induced cellular
dysfunction. Developing strategies to detect the amyloids at an early
stage of development and to assess the induced cellular damage are crucial
for diagnosis and treatment of protein conformational diseases, such as
Alzheimers disease, type 2 diabetes mellitus and diabetic cardiomyopathy.
Cost: FREE
Sponsored by: WPI Physics Department, Dr. Izabela Stroe
Suggested Audiences: College
E-mail:
izabela@wpi.edu
Phone: 508-831-5249
Last Modified: March 23, 2009 at 2:33 PM
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