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Type: Artigo de periódico
Title: Mapping the Intramolecular Vibrational Energy Flow in Proteins Reveals Functionally Important Residues
Author: MARTINEZ, Leandro
WEBB, Paul
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.
Country: Estados Unidos
Citation: JOURNAL OF PHYSICAL CHEMISTRY LETTERS, v.2, n.16, p.2073-2078, 2011
Rights: fechado
Identifier DOI: 10.1021/jz200830g
Date Issue: 2011
Appears in Collections:IQ - Artigos e Outros Documentos

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