Literature DB >> 18232827

Hydrodynamic description of protein folding.

Sergei F Chekmarev1, Andrey Yu Palyanov, Martin Karplus.   

Abstract

A hydrodynamic description of protein folding is proposed and illustrated with a lattice protein model, which has a free energy surface (FES) typical of proteins with two-state folding kinetics. The flows from the unfolded to the native state are concentrated in a limited region of the FES. The rest is occupied by a flow "vortex", which does not lead to the native state. In contrast with intermediates that are associated with local minima, the vortex is not visible on the FES. The hydrodynamic interpretation thus provides new insights into the mechanism of protein folding and can be a useful complement to standard analyses.

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Year:  2008        PMID: 18232827     DOI: 10.1103/PhysRevLett.100.018107

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  8 in total

1.  A hydrodynamic view of the first-passage folding of Trp-cage miniprotein.

Authors:  Vladimir A Andryushchenko; Sergei F Chekmarev
Journal:  Eur Biophys J       Date:  2015-11-12       Impact factor: 1.733

2.  Individual-based modelling: an essential tool for microbiology.

Authors:  Jordi Ferrer; Clara Prats; Daniel López
Journal:  J Biol Phys       Date:  2008-07-19       Impact factor: 1.365

3.  Temperature evolution of Trp-cage folding pathways: An analysis by dividing the probability flux field into stream tubes.

Authors:  Vladimir A Andryushchenko; Sergei F Chekmarev
Journal:  J Biol Phys       Date:  2017-10-05       Impact factor: 1.365

4.  New insights into the folding of a β-sheet miniprotein in a reduced space of collective hydrogen bond variables: application to a hydrodynamic analysis of the folding flow.

Authors:  Igor V Kalgin; Amedeo Caflisch; Sergei F Chekmarev; Martin Karplus
Journal:  J Phys Chem B       Date:  2013-05-15       Impact factor: 2.991

5.  Impact of hydrodynamic interactions on protein folding rates depends on temperature.

Authors:  Fabio C Zegarra; Dirar Homouz; Yossi Eliaz; Andrei G Gasic; Margaret S Cheung
Journal:  Phys Rev E       Date:  2018-03       Impact factor: 2.529

6.  Protein folding as a complex reaction: a two-component potential for the driving force of folding and its variation with folding scenario.

Authors:  Sergei F Chekmarev
Journal:  PLoS One       Date:  2015-04-07       Impact factor: 3.240

7.  Turbulence in protein folding: Vorticity, scaling and diffusion of probability flows.

Authors:  Vladimir A Andryushchenko; Sergei F Chekmarev
Journal:  PLoS One       Date:  2017-12-05       Impact factor: 3.240

8.  First passage analysis of the folding of a β-sheet miniprotein: is it more realistic than the standard equilibrium approach?

Authors:  Igor V Kalgin; Sergei F Chekmarev; Martin Karplus
Journal:  J Phys Chem B       Date:  2014-04-09       Impact factor: 2.991

  8 in total

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