The standard coil or globule phases cannot describe the denatured state of structured proteins and intrinsically disordered proteins

The concepts of globule and random coil were developed to describe the phases of homopolymers and then used to characterize the denatured state of structured cytosolic proteins and intrinsically disordered proteins. Using multi-scale molecular dynamics simulations, we were able to explore the conformational space of the disordered conformations of both types of protein under biological conditions in an affordable amount of computational time. By studying the size of the protein and the density correlations in space, we conclude that the standard phases of homopolymers and the tools to detect them cannot be applied straightforwardly to proteins.

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Publication Details

Journal
The Journal of Chemical Physics
Published
2025-04-01
DOI
https://doi.org/10.1063/5.0257525
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
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article

The standard coil or globule phases cannot describe the denatured state of structured proteins and intrinsically disordered proteins

Riccardo Capelli, G. Potel, F. Righini, Guido Tiana
The Journal of Chemical Physics
Protein Structure and Dynamics
article

The standard coil or globule phases cannot describe the denatured state of structured proteins and intrinsically disordered proteins

Riccardo Capelli, G. Potel, F. Righini, Guido Tiana
article en

Abstract

The concepts of globule and random coil were developed to describe the phases of homopolymers and then used to characterize the denatured state of structured cytosolic proteins and intrinsically disordered proteins. Using multi-scale molecular dynamics simulations, we were able to explore the conformational space of the disordered conformations of both types of protein under biological conditions in an affordable amount of computational time. By studying the size of the protein and the density correlations in space, we conclude that the standard phases of homopolymers and the tools to detect them cannot be applied straightforwardly to proteins.

The Journal of Chemical PhysicsVol. 162(13)
Lawrence Livermore National Laboratory (US), University of Milan (IT), Istituto Nazionale di Fisica Nucleare, Sezione di Milano (IT)
Openalex Percentile: Top 94%
Protein Structure and Dynamics
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