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Pervasive, conserved secondary structure in highly charged protein regions
Catherine G Triandafillou1, Rosalind Wenshan Pan2, Aaron R Dinner3
1Department of Bioengineering, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
Plos Computational Biology
|October 16, 2023
Summary
Highly charged protein regions, often assumed disordered, frequently form stable helical structures. This finding challenges traditional views and highlights the need to integrate structure and disorder in protein research.
Area of Science:
- Molecular Biology
- Structural Biology
- Biophysics
Background:
- Protein function is dictated by sequence, but understanding this link is challenging.
- Structure-based and disorder-based approaches are often studied separately.
- Highly charged protein regions are typically presumed to be intrinsically disordered.
Purpose of the Study:
- To investigate the structural properties of highly charged protein regions (>40% charged residues).
- To determine the prevalence of stable structures within these regions.
- To challenge the assumption that high charge equates to intrinsic disorder.
Main Methods:
- Utilized recent advances in protein structure prediction tools.
- Analyzed experimentally determined protein structures.
- Developed and tested a composition-based classifier for structure prediction.
- Evaluated traditional disorder prediction heuristics (charge, hydropathy).
Main Results:
- Approximately 40% of highly charged protein regions form well-defined helical structures.
- Commonly cited disorder predictors (high charge, low hydrophobicity) are compatible with helical structures.
- A simple composition classifier outperformed traditional methods in predicting structure.
- Helical structures are more prevalent in charged regions across diverse proteomes than previously thought.
Conclusions:
- Highly charged protein regions can adopt stable helical structures.
- The dichotomy between structure- and disorder-based approaches is artificial for these regions.
- Integrating structure and disorder perspectives is crucial for a comprehensive understanding of protein function.
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