On hydrodynamic interpretation of folding of an О±-helical protein
V.A. Andryushchenko1,2 and S.F. Chekmarev1,2
1 Kutateladze Institute of Thermophysics SB RAS, Novosibirsk, Russia
2 Novosibirsk State University, Novosibirsk, Russia
E-mail: chekmarev@itp.nsc.ru
Keywords: О±-helical protein, folding, folding flux, turbulence
Pages: 941–944
Abstract
Using the method of molecular dynamics,
the simulation of folding of an α-helical protein
from the unfolded to compact and functional (native) state is performed.
The protein folding is interpreted as a stationary motion of
a compressible “folding fluid”. It is shown that the densities of
folding fluxes obey the same similarity relations as the velocities
of an incompressible fluid in the Kolmogorov’s turbulence theory,
except that instead of the rate of change of kinetic energy per mass unit,
the rate of change of flux variance per volume unit plays the role of
the key parameter.
DOI: 10.1134/S0869864316060184
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