About
the Featured Image
The role
of dynamics in the biological function of proteins and enzymes
has been a topic of intense debate for decades. The use of
vibrational spectroscopy, the most direct method to study
dynamics, has been limited by the congestion of the protein
vibrational spectrum. Floyd Romesberg, assistant professor
of chemistry at the Scripps Research Institute, and his colleagues
use cytochrome c as a model system to demonstrate that individual
protein vibrations may be directly observed by the incorporation
of an isotopically labeled amino acid, and that those labeled
vibrations are sensitive probes of the protein environment.
This volume-rendered image shows a model that was investigated
with computational quantum chemical methods, for the Fe (II)-
and Fe (III)- cytochrome c prosthetic group, revealing the
structure and specific vibrational properties of the FeP (DMS)
complex, which were then compared to experimentally generated
data.
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