Intra-protein interacting collective modes in the terahertz frequency region

Abstract

Understanding how proteins work requires a thorough understanding of their internal dynamics. Proteins support a wide range of motions, from the femtoseconds to seconds time scale, relevant to crucial biological functions. In this context, the term “protein collective dynamics” refers to the complex patterns of coordinated motions of numerous atoms throughout the protein in the sub-picosecond time scale (terahertz frequency region). It is hypothesized that these dynamics have a substantial impact on the regulation of functional dynamical mechanisms, including ligand binding and allosteric signalling, charge transport direction, and the regulation of thermodynamic and thermal transport properties. Using the theoretical framework of hydrodynamics, the collective dynamics of proteins had previously been described in a manner akin to that of simple liquids, i.e. in terms of a single acoustic-like excitation, related to intra-protein vibrational motions. Here, we employ an interacting-mode model to analyse the results from molecular dynamics simulations and we unveil that the vibrational landscape of proteins is populated by multiple acoustic-like and low-frequency optic-like modes, with mixed symmetry and interfering with each other. We propose an interpretation at the molecular level of the observed scenario that we relate to the side-chains and the hydrogen-bonded networks dynamics. The present insights provide a perspective for understanding the molecular mechanisms underlying the energy redistribution processes in the interior of proteins.

Dynamical Transition in Dehydrated Proteins

“…They hypothesize that anharmonic interactions and therefore the interactions between modes play an important role in the thermal transport as well as in the regulation of functional dynamical mechanisms. 13 Instead of studying solvated biomolecules, we implemented an extensive lyophilization process to remove as many water molecules as possible from protein samples. We can thus study protein dynamics decoupled from solvent effects.…”

“…They found multiple interfering acoustic-like and low-frequency optic-like modes, which suggest that protein collective dynamics are very complex. They hypothesize that anharmonic interactions and therefore the interactions between modes play an important role in the thermal transport as well as in the regulation of functional dynamical mechanisms …”

“…They hypothesize that anharmonic interactions and therefore the interactions between modes play an important role in the thermal transport as well as in the regulation of functional dynamical mechanisms. 13 …”