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Photo Marie Skepö

Marie Skepö

Professor

Photo Marie Skepö

Glutenin and gliadin, a piece in the puzzle of their structural properties in the cell described through monte carlo simulations

Author

  • Joel Markgren
  • Mikael Hedenqvist
  • Faiza Rasheed
  • Marie Skepö
  • Eva Johansson

Summary, in English

Gluten protein crosslinking is a predetermined process where specific intra-and intermolecular disulfide bonds differ depending on the protein and cysteine motif. In this article, all-atom Monte Carlo simulations were used to understand the formation of disulfide bonds in gliadins and low molecular weight glutenin subunits (LMW-GS). The two intrinsically disordered proteins appeared to contain mostly turns and loops and showed “self-avoiding walk” behavior in water. Cysteine residues involved in intramolecular disulfide bonds were located next to hydrophobic peptide sections in the primary sequence. Hydrophobicity of neighboring peptide sections, synthesis chronology, and amino acid chain flexibility were identified as important factors in securing the specificity of intramolecular disulfide bonds formed directly after synthesis. The two LMW-GS cysteine residues that form intermolecular disulfide bonds were positioned next to peptide sections of lower hydrophobicity, and these cysteine residues are more exposed to the cytosolic conditions, which influence the crosslinking behavior. In addition, coarse-grained Monte Carlo simulations revealed that the protein folding is independent of ionic strength. The potential molecular behavior associated with disulfide bonds, as reported here, increases the biological understanding of seed storage protein function and provides opportunities to tailor their functional properties for different applications.

Department/s

  • Computational Chemistry
  • eSSENCE: The e-Science Collaboration

Publishing year

2020

Language

English

Publication/Series

Biomolecules

Volume

10

Issue

8

Document type

Journal article

Publisher

MDPI AG

Topic

  • Biological Sciences

Keywords

  • Cysteine
  • Disulfide bonds
  • Gluten
  • Intrinsically disordered proteins
  • Modeling
  • Monte Carlo
  • Prolamin

Status

Published

ISBN/ISSN/Other

  • ISSN: 2218-273X