On hydrodynamic interpretation of folding of an α-helical protein
- Autores: Andryushchenko V.1, Chekmarev S.1,2
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Afiliações:
- Kutateladze Institute of Thermophysics SB RAS
- Novosibirsk State University
- Edição: Volume 23, Nº 6 (2016)
- Páginas: 941-944
- Seção: Brief Communications
- URL: https://journals.rcsi.science/1531-8699/article/view/216813
- DOI: https://doi.org/10.1134/S0869864316060184
- ID: 216813
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Resumo
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.
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Sobre autores
V. Andryushchenko
Kutateladze Institute of Thermophysics SB RAS
Email: chekmarev@itp.nsc.ru
Rússia, Novosibirsk
S. Chekmarev
Kutateladze Institute of Thermophysics SB RAS; Novosibirsk State University
Autor responsável pela correspondência
Email: chekmarev@itp.nsc.ru
Rússia, Novosibirsk; Novosibirsk