Allosteric communication pathways and thermal rectification in pdz-2 protein: A computational study

Germán A. Miño-Galaz

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


Allosteric 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.

Original languageEnglish
Pages (from-to)6179-6189
Number of pages11
JournalJournal of Physical Chemistry B
Issue number20
Publication statusPublished - 21 May 2015
Externally publishedYes

ASJC Scopus subject areas

  • Surfaces, Coatings and Films
  • Physical and Theoretical Chemistry
  • Materials Chemistry


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