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|Title:||Mapping the intramolecular vibrational energy flow in proteins reveals functionally important residues|
Figueira, Ana C. M.
Skaf, Munir S.
|Abstract:||Unveiling the mechanisms of energy relaxation in biomolecules is key to our understanding of protein stability, allostery, intramolecular signaling, and long-lasting quantum coherence phenomena at ambient temperatures. Yet, the relationship between the pathways of energy transfer and the functional role of the residues involved remains largely unknown. Here, we develop a simulation method of mapping out residues that are highly efficient in relaxing an initially localized excess vibrational energy and perform site-directed mutagenesis functional assays to assess the relevance of these residues to protein function. We use the ligand binding domains of thyroid hormone receptor (TR) subtypes as a test case and find that conserved arginines, which are critical to TR transactivation function, are the most effective heat diffusers across the protein structure. These results suggest a hitherto unsuspected connection between a residue’s ability to mediate intramolecular vibrational energy redistribution and its functional relevance|
|Editor:||American Chemical Society|
|Appears in Collections:||IQ - Artigos e Outros Documentos|
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