Molecular Modeling of Unusual Spiral Structure in Elastomeric Wheat Seed Protein

Parchment, Oswald G.; Shewry, Peter R.; Tatham, Arthur S.; Osguthorpe, David J.

doi:10.1094/cchem.2001.78.6.658

Cited by 18 publications

(13 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the sample preparation procedures used prevented the study from validating the existence of the β-spiral in bulk gluten. Models of single glutenin structures consisting of repetitive β [59] and γ [10] turns were reported in the literature, however we did not observe similar structures in our simulations.…”

Section: Resultscontrasting

confidence: 52%

Viscoelastic properties of wheat gluten in a molecular dynamics study

Mioduszewski

Cieplak

2020

Preprint

View full text Add to dashboard Cite

Wheat (Triticum spp.) gluten consists mainly of intrinsincally disordered storage proteins (glutenins and gliadins) that can form megadalton-sized networks. These networks are responsible for the unique viscoelastic properties of wheat dough and affect the quality of bread. These properties have not yet been studied by molecular level simulations. Here, we use a newly developed α-C-based coarse-grained model to study ∼ 4000-residue systems. The corresponding time-dependent properties are studied through shear and axial deformations. We measure the response force to the deformation, the number of entanglements and cavities, the size of fluctuations, the number of the inter-chain bonds, etc. Glutenins are shown to influence the mechanics of gluten much more than gliadins. Our simulations are consistent with the existing ideas about gluten elasticity and emphasize the role of entanglements and hydrogen bonding. We also demonstrate that the storage proteins in maize and rice lead to weaker elasticity which points to the unique properties of wheat gluten.

show abstract

Section: Resultscontrasting

confidence: 52%

Viscoelastic properties of wheat gluten in a molecular dynamics study

Mioduszewski

Cieplak

2020

Preprint

View full text Add to dashboard Cite

show abstract

“…Likewise, the mobile regions observed by NMR are associated with b-turn structures observed by FT-IR. The most plausible explanation would be that they adopt the solventaccessible, relatively loose structure of the proposed b-spiral (Parchment et al 2001). Given the dynamic nature of the structures adopted by the repetitive domains of prolamins, it is currently not possible to tell whether the b-spiral comprises only specific parts or whole domains.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, these data suggest that the chaotropic Ianions reduced the intermolecular b-sheet content, but the resulting solubilized form of the protein was not random but characterized predominantly by b-turns. This soluble form of prolamins may adopt a b-spiral structure (Parchment et al 2001) that does not appear to rely on hydrogen bonds for stabilization. To compare the effects of different salt concentrations on the secondary structure, the relative intensities at four characteristic wavenumbers (1,620, 1,630, 1,650, and 1,666 cm -1 ) were plotted.…”

Section: H Nmr Relaxationmentioning

confidence: 99%

Effect of Selected Hofmeister Anions on the Secondary Structure and Dynamics of Wheat Prolamins in Gluten

et al. 2003

View full text Add to dashboard Cite

The effect of selected salts (NaCl, NaBr, NaI) with increasingly chaotropic anions on gluten prolamin secondary structure and dynamics was studied using FT-IR and NMR spectroscopy. FT-IR spectra indicated a small increase in intermolecular ß-sheet structures when gluten samples were incubated with low levels of NaCl and NaBr. The ß-sheet content remained constant with further NaCl addition, but was reduced again with higher NaBr concentrations. NaI addition generally reduced the amount of ß-sheet and increased the amount of ß-turns. From these data, it could be concluded that, in the presence of chaotropic anions, the proteins tended to prefer the ß-turn helix structure characteristic of glutenin subunits in solution. 1H-NMR relaxation showed that the molecules were more rigid in 1M NaCl than in pure water, and that the mobility of the prolamins in the presence of 1M NaCl, NaBr, and NaI increased in accordance with the position of the anions in the Hofmeister series. The increase in mobility appeared to be associated with the increase in ß-turn helical structures

show abstract

“…3b. It was noticed from the results that good variety HI 977 had more pronounced b-turn intensity at 1665 cm -1 indicating that glutenin fraction was very rich in b-turns (Parchment et al 2001). b-turn structure of HMW-GS organize to give a regular b-spiral structure.…”

Section: Ir Spectroscopy Characterisation Of Gluten and Its Fractionsmentioning

confidence: 95%

Microstructural, thermal and IR spectroscopy characterisation of wheat gluten and its sub fractions

Dhaka

Khatkar

2016

J Food Sci Technol

View full text Add to dashboard Cite

The gluten and its sub-fractions of good and poor bread quality wheat varieties were studied using scanning electron microscopy, differential scanning calorimetry (DSC) and IR spectroscopy techniques. The gluten of good bread quality wheat variety showed organized foam like matrix, whereas that of poor demonstrated an open gluten matrix. The glutenin of good bread quality wheat (HI 977) exhibited a more striated, organised texture in contrast to a dense, unorganised structure visible in C306. Gliadins of poor bread quality wheat were selfassembled to form a sheet like structure, whereas the gliadin proteins of good bread quality wheat variety showed more open microstructure. DSC thermal profiles of gluten and glutenin proteins of poor bread quality wheat showed exothermic peaks at around 200°C. A distinct endothermic peak was detected in the glutenin fraction of good bread quality wheat, suggesting greater thermostability. Amide I peak at *1668 cm -1 for gluten of good bread quality wheat variety showed higher relative intensities of b-turn as compared to observed for gluten of poor bread quality.

show abstract

Molecular Modeling of Unusual Spiral Structure in Elastomeric Wheat Seed Protein

Cited by 18 publications

References 24 publications

Viscoelastic properties of wheat gluten in a molecular dynamics study

Viscoelastic properties of wheat gluten in a molecular dynamics study

Effect of Selected Hofmeister Anions on the Secondary Structure and Dynamics of Wheat Prolamins in Gluten

Microstructural, thermal and IR spectroscopy characterisation of wheat gluten and its sub fractions

Contact Info

Product

Resources

About