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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.