Ensemble-Biased Disulfide Chemistry Orchestrates the Multidimensional Gluten Network Topology
Boyu Xie1, Jihui Gao1, Jiahui Fu1
1Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China.
Journal of the American Chemical Society
|July 15, 2026
Summary
Wheat dough
Area of Science:
- Biochemistry
- Materials Science
- Food Science
Background:
- Wheat flour transforms into dough upon hydration due to glutenin polymerization.
- The molecular mechanisms behind this dough formation are not fully understood.
Purpose of the Study:
- Investigate the hydration-induced association of the N-terminal domain of high-molecular-weight glutenin subunit 1Dx5 (1Dx5-NTD).
- Elucidate the molecular principles governing glutenin polymerization and dough formation.
Main Methods:
- Investigated 1Dx5-NTD hydration and association behavior.
- Utilized mutational analysis to study the role of hydrophobic residues.
- Employed mass spectrometry-based cross-linking to analyze disulfide bond formation.
Main Results:
- Hydrated 1Dx5-NTD forms a heterogeneous ensemble, not a single structure.
- Intermolecular association occurs, forming large assemblies driven by enthalpic interactions.
- Disulfide bond formation is preferential, not random, influenced by conformational ensemble and cysteine accessibility.
Conclusions:
- Glutenin polymerization arises from ensemble-averaged contacts and biased disulfide formation.
- A cohesive protein network forms without a single defined structure.
- Collapsed protein ensembles can dictate material properties and chemical selectivity.
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