Title of Paper:The hydrogen-bond configuration modulates the energy transfer efficiency in helical protein nanotubes

Journal:Nanoscale

Summary:Energy transport in proteins is critical to a variety of physical, chemical, and biological processes in living organisms. While strenuous efforts have been made to study vibrational energy transport in proteins, thermal transport processes across the most fundamental building blocks of proteins, i.e. helices, are not well understood. This work studies energy transport in a group of “isomer” helices. The π-helix is shown to have the highest thermal conductivity, 110% higher than that of the α-helix and 207% higher than that of the 310-helix. The H-bond connectivity is found to govern thermal transport mechanisms including the phonon spectral energy density, dispersion, mode-specific transport, group velocity, and relaxation time. The energy transport is strongly correlated with the H-bond strength which is also modulated by the H-bond connectivity. These fundamental insights provide a novel perspective for understanding energy transfer in proteins and guiding a rational molecule-level design of novel materials with configurable H-bonds.

First Author:Jinlong He, Lin Zhang, Ling Liu*

Document Code:CA84BAC8587D4CFEAD864BA37A76C396

Discipline:Engineering

Volume:13

Issue:2

Page Number:991-999

Impact Factor:7.79

DOI Number:10.1039/D0NR06031C

Number of Words:8

Translation or Not:No

Date of Publication:2021-05

Included Journals:SCI

Release Time:2021-10-23