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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Partially Globular Conformations from Random Charge Sequences.

Min-Kyung Chae¹, Nam-Kyung Lee¹, Youngkyun Jung²

¹Department of Physics and Astronomy, Sejong University, Seoul 05006, Korea.

ACS Macro Letters

|May 16, 2022

Summary

This summary is machine-generated.

Charged polymers form globular structures due to disordered sequences and fluctuations. Favorable structures contain large, undercharged globules and many small, overcharged ones, revealing emergent order in polymer science.

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Area of Science:

Polymer Physics
Soft Matter Physics

Background:

Charged polymers with disordered sequences often form partially globular structures.
These structures arise from the interplay of sequence disorder and thermal fluctuations.
Homogeneous globules (equal size and charge) are energetically unfavorable.

Purpose of the Study:

To predict the most stable globule distributions in size-charge space for charged polymers.
To investigate the emergence of order in quenched random charge sequences.
To validate theoretical energy models with simulation data.

Main Methods:

Theoretical prediction of low-energy globule distributions.
Large-scale molecular dynamics simulations of quenched random +/- sequences.
Analysis of globule size and charge distributions.

Main Results:

Favorable structures consist of a mix of large (undercharged) and small (overcharged) globules.
Simulations confirm that random sequences adopt these predicted low-energy states.
Emergent order is observed in the distribution of globule sizes, validating the energy model.

Conclusions:

Charged polymers exhibit an emergent order in their globular structures, favoring specific size-charge distributions.
The theoretical energy model accurately predicts the structures observed in molecular dynamics simulations.
Findings have implications for understanding polyampholytes, polyelectrolytes, and intrinsically disordered proteins.