LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

Protein Folding Dynamics in the Space of Experimentally Measured Variables: Turbulence Phenomena

Photo from wikipedia

The process of folding of villin subdomain HP-35 has been studied using the method of molecular dynamics. To characterize protein conformations, two variables are introduced that correspond to the distances… Click to show full abstract

The process of folding of villin subdomain HP-35 has been studied using the method of molecular dynamics. To characterize protein conformations, two variables are introduced that correspond to the distances between fluorophores in experiments on protein folding with the Förster resonance energy. The simulation results show that the field of probability flows of transitions between protein states is filled with eddies. It has been found that, in contrast to the previously studied cases of hydrodynamic turbulence and turbulence in protein folding in three-dimensional conformational space, the structure functions of the flows of various orders depend linearly on the increment in the conformational space. An explanation of this linear dependence based on the β-model is proposed. It is shown that this dependence is not due to the choice of variables to describe the folding process.

Keywords: turbulence; protein folding; space experimentally; folding dynamics; dynamics space

Journal Title: Journal of Applied Mechanics and Technical Physics
Year Published: 2018

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.