Miño-Galaz, Germán A.2023-05-312023-05-312015-05Journal of Physical Chemistry B Volume 119, Issue 20, Pages 6179 - 618921 May 20151520-6106https://repositorio.unab.cl/xmlui/handle/ria/50182Indexación: ScopusAllosteric communication in proteins is a fundamental and yet unresolved problem of structural biochemistry. Previous findings, from computational biology (Ota, N.; Agard, D. A. J. Mol. Biol. 2005, 351, 345?354), have proposed that heat diffuses in a protein through cognate protein allosteric pathways. This work studied heat diffusion in the well-known PDZ-2 protein, and confirmed that this protein has two cognate allosteric pathways and that heat flows preferentially through these. Also, a new property was also observed for protein structures: heat diffuses asymmetrically through the structures. The underling structure of this asymmetrical heat flow was a normal length hydrogen bond (?2.85 Å) that acted as a thermal rectifier. In contrast, thermal rectification was compromised in short hydrogen bonds (?2.60 Å), giving rise to symmetrical thermal diffusion. Asymmetrical heat diffusion was due, on a higher scale, to the local, structural organization of residues that, in turn, was also mediated by hydrogen bonds. This asymmetrical/symmetrical energy flow may be relevant for allosteric signal communication directionality in proteins and for the control of heat flow in materials science. © 2015 American Chemical Society.enMolecular RelaxationInfrared SpectroscopyMolecular DynamicsArtículoAtribución 4.0 Internacional (CC BY 4.0)10.1021/acs.jpcb.5b02228