Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-07-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/8/1095 |
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| author | Joel Markgren Mikael Hedenqvist Faiza Rasheed Marie Skepö Eva Johansson |
| author_facet | Joel Markgren Mikael Hedenqvist Faiza Rasheed Marie Skepö Eva Johansson |
| author_sort | Joel Markgren |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T18:15:44Z |
| format | Article |
| id | doaj.art-38712d4cabbe430892648884b51ea568 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T18:15:44Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-38712d4cabbe430892648884b51ea5682023-11-20T07:42:11ZengMDPI AGBiomolecules2218-273X2020-07-01108109510.3390/biom10081095Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo SimulationsJoel Markgren0Mikael Hedenqvist1Faiza Rasheed2Marie Skepö3Eva Johansson4Department of Plant Breeding, Swedish University of Agricultural Sciences, P.O. Box 101, SE-230 53 Alnarp, SwedenDepartment of Fibre and Polymer Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-100 44 Stockholm, SwedenDepartment of Fibre and Polymer Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-100 44 Stockholm, SwedenTheoretical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, SwedenDepartment of Plant Breeding, Swedish University of Agricultural Sciences, P.O. Box 101, SE-230 53 Alnarp, SwedenGluten 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.https://www.mdpi.com/2218-273X/10/8/1095modelingintrinsically disordered proteinsglutendisulfide bondscysteineprolamin |
| spellingShingle | Joel Markgren Mikael Hedenqvist Faiza Rasheed Marie Skepö Eva Johansson Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations Biomolecules modeling intrinsically disordered proteins gluten disulfide bonds cysteine prolamin |
| title | Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations |
| title_full | Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations |
| title_fullStr | Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations |
| title_full_unstemmed | Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations |
| title_short | Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations |
| title_sort | glutenin and gliadin a piece in the puzzle of their structural properties in the cell described through monte carlo simulations |
| topic | modeling intrinsically disordered proteins gluten disulfide bonds cysteine prolamin |
| url | https://www.mdpi.com/2218-273X/10/8/1095 |
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