Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348478
Type: Outro documento
Title: Mapping the intramolecular vibrational energy flow in proteins reveals functionally important residues
Author: Martínez, Leandro
Figueira, Ana C. M.
Webb, Paul
Polikarpov, Igor
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
Subject: Termodifusão
Country: Estados Unidos
Editor: American Chemical Society
Rights: Fechado
Identifier DOI: 10.1021/jz200830g
Address: https://pubs.acs.org/doi/10.1021/jz200830g
Date Issue: 2011
Appears in Collections:IQ - Artigos e Outros Documentos

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