Comment on “Main role of fractal-like nature of conformational space in subdiffusion in proteins”

Maggi and Orozco [Phys. Rev. E 109, 034402 (2024)10.1103/PhysRevE.109.034402] address the question of the origin of the subdiffusional dynamics observed in molecular dynamics (MD) simulations of proteins. Confirming the conclusions of previous publications that used closely similar methods [Neusius et al. Phys. Rev. Lett. 100, 188103 (2008)10.1103/PhysRevLett.100.188103; Phys. Rev. E 83, 021902 (2011)10.1103/PhysRevE.83.021902], Maggi and Orozco conclude that a random walk on a fractal surface is an appropriate model. However, the logic used in their paper to make that conclusion is erroneous.

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Publication Details

Journal
Physical review. E
Published
2025-05-09
DOI
https://doi.org/10.1103/physreve.111.056401
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
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article

Comment on “Main role of fractal-like nature of conformational space in subdiffusion in proteins”

Jeremy C. Smith, Igor M. Sokolov, Thomas Neusius
Physical review. E
Protein Structure and Dynamics
article

Comment on “Main role of fractal-like nature of conformational space in subdiffusion in proteins”

Jeremy C. Smith, Igor M. Sokolov, Thomas Neusius
article en

Abstract

Maggi and Orozco [Phys. Rev. E 109, 034402 (2024)10.1103/PhysRevE.109.034402] address the question of the origin of the subdiffusional dynamics observed in molecular dynamics (MD) simulations of proteins. Confirming the conclusions of previous publications that used closely similar methods [Neusius et al. Phys. Rev. Lett. 100, 188103 (2008)10.1103/PhysRevLett.100.188103; Phys. Rev. E 83, 021902 (2011)10.1103/PhysRevE.83.021902], Maggi and Orozco conclude that a random walk on a fractal surface is an appropriate model. However, the logic used in their paper to make that conclusion is erroneous.

Physical review. EVol. 111(5)
Oak Ridge National Laboratory (US), Humboldt-Universität zu Berlin (DE), RheinMain University of Applied Sciences (DE), University of Tennessee at Knoxville (US)
Openalex Percentile: Top 91%
Protein Structure and Dynamics
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