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Updated: Aug 5, 2025
11:14
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
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The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins
Jhullian J Alston1,2, Garrett M Ginell1,2, Andrea Soranno1,2
1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
Biorxiv : the Preprint Server for Biology
|March 30, 2023
Summary
A new analytical polymer model, the analytical Flory Random Coil (AFRC), uses amino acid sequences to predict unfolded protein conformations. This provides a reference for interpreting experimental and simulation data of disordered proteins.
Area of Science:
- Biophysics
- Computational Biology
- Polymer Physics
Background:
- Analytical polymer models describe unfolded proteins but often require manual parameterization.
- A standardized, sequence-input model is needed for interpreting disordered protein data.
Approach:
- Utilized all-atom simulations and polymer scaling theory to parameterize an analytical model for unfolded polypeptides.
- Developed the analytical Flory Random Coil (AFRC) model, treating polypeptides as ideal chains (ν = 0.50).
Key Points:
- The AFRC model requires only the amino acid sequence as input.
- It provides direct access to conformational order parameter distributions.
- The model establishes a reference state for normalizing experimental and simulation results.
Conclusions:
- The AFRC model aids in identifying sequence-specific intramolecular interactions in disordered proteins.
- It successfully contextualizes experimental data, such as radii of gyration from SAXS.
- The AFRC offers a user-friendly reference polymer model for biophysical research.
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