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Published on: July 16, 2017
Mapping the Conformational Landscape of the Cold-Regulated Intrinsically Disordered Protein COR15A
Dale Stuchfield1, Ana Bath Alén1, Matthew Venables1
1Manchester Institute of Biotechnology, University of Manchester, Oxford Road, ManchesterM13 9PL, U.K.
The Journal of Physical Chemistry. B
|August 6, 2026
Summary
Arabidopsis thaliana's COR15A protein, a key player in cold and dehydration responses, was studied using ion mobility-mass spectrometry and molecular dynamics simulations. This revealed two main protein structures, offering insights into plant stress adaptation.
Area of Science:
- Plant molecular biology
- Biophysics
- Structural biology
Background:
- Late embryogenesis abundant (LEA) proteins, such as COR15A from Arabidopsis thaliana, are crucial for plant tolerance to abiotic stresses like cold and dehydration.
- Understanding the conformational dynamics of LEA proteins is essential for elucidating their protective mechanisms.
Purpose of the Study:
- To explore the conformational landscape of COR15A using a combination of experimental and computational techniques.
- To investigate the structural basis of COR15A's function under stress conditions.
Main Methods:
- Ion mobility-mass spectrometry (IM-MS) was employed to analyze protein charge states and collision cross section (CCS) distributions.
- Molecular dynamics (MD) simulations at elevated temperatures were used for enhanced conformational sampling.
- Comparison of experimental IM-MS data with MD-derived pseudo-CCS distributions and small-angle X-ray scattering (SAXS) data.
Main Results:
- IM-MS data revealed two dominant coexisting conformational families of COR15A, with CCS values centered around 1200 Ų and 1800 Ų, along with evidence of subconformers.
- MD simulations successfully reproduced the experimental IM-MS data, validating the sampled conformations as natively accessible states.
- The study demonstrated that IM-MS can simultaneously observe disordered and dehydration-populated conformers, providing a comprehensive view of LEA protein behavior.
Conclusions:
- The combined IM-MS and MD approach provides a powerful tool for characterizing the conformational heterogeneity of intrinsically disordered proteins like COR15A.
- The findings offer critical insights into how LEA proteins maintain structure and function under dehydration stress, contributing to plant survival.
- This study highlights the utility of IM-MS in studying protein conformations relevant to functional states, including those encountered during dehydration.
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