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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

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Evolution of function in the "two dinucleotide binding domains" flavoproteins

Sunil Ojha1, Elaine C Meng, Patricia C Babbitt

  • 1Department of Biopharmaceutical Sciences, University of California San Francisco, San Francisco, California, USA.

Plos Computational Biology
|July 31, 2007
PubMed
Summary

The conserved structure of cofactors in flavoproteins (tDBDF) dictates electron flow and protein interactions, driving functional evolution. This structural constraint enables diverse protein partners to bind, leading to new molecular functions.

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