Science / Technology - Colloquium
Wednesday, November 19, 2008
4:00 PM-5:00 PM
Olin Hall
223
Proteins are complex systems that connect biology, biophysics, biochemistry, chemistry, physics,
and even mathematics. Proteins share similarities with supercooled liquids and glasses, such
frustration, the existence of an energy landscape, and alpha and beta fluctuations. Protein are,
however, far more complex than glasses and they can be modified and studied in much more detail.
Protein research therefore has not only impact in the life sciences, but also in other fields.
The beautiful pictures of protein structures that appear in many publications often create the
impression that proteins are rigid and function independently of their environment. Proteins are,
however, surrounded by hydration water and they are embedded in a bulk solvent. The motions in the
hydration shell and the bulk solvent actually control the internal protein motions. Experiments
with myoglobin that separately monitor the external and internal fluctuations show that the alpha
fluctuations of the bulk solvent drive the large-scale protein motions and that the beta
fluctuations of the hydration water drive the internal protein motions. These results hint that
the protein surface is functionally as important as the interior. The data also prove that there
is no dynamic transition or "fragile-to-strong transition" near 200 K in proteins.
Cost: FREE
Sponsored by: WPI Physics Department, Dr. Izabela Stroe
Suggested Audiences: College, Adult
E-mail:
izabela@wpi.edu
Phone: 508-831-5249
Last Modified: November 5, 2008 at 9:42 AM
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