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|Type:||Artigo de periódico|
|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:||AMER CHEMICAL SOC|
|Citation:||JOURNAL OF PHYSICAL CHEMISTRY LETTERS, v.2, n.16, p.2073-2078, 2011|
|Appears in Collections:||IQ - Artigos e Outros Documentos|
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|art_MARTINEZ_Mapping_the_Intramolecular_Vibrational_Energy_Flow_in_2011.pdf||published version||903.58 kB||Adobe PDF||View/Open|
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