Mioduszewski Łukasz, Cieplak Marek
Institute of Physics, Polish Academy of Sciences, Warsaw, Poland.
PLoS Comput Biol. 2021 Mar 24;17(3):e1008840. doi: 10.1371/journal.pcbi.1008840. eCollection 2021 Mar.
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 mobility of residues, 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.
小麦（Triticum spp.）面筋主要由内在无序的贮藏蛋白（谷蛋白和醇溶蛋白）组成，这些蛋白可形成兆道尔顿大小的网络。这些网络决定了小麦面团独特的粘弹性，并影响面包的品质。尚未通过分子水平模拟研究这些特性。在此，我们使用新开发的基于α-C的粗粒化模型来研究约4000个残基的系统。通过剪切和轴向变形研究相应的时间相关特性。我们测量对变形的响应力、缠结和空洞的数量、残基的迁移率、链间键的数量等。结果表明，谷蛋白对面筋力学的影响远大于醇溶蛋白。我们的模拟与关于面筋弹性的现有观点一致，并强调了缠结和氢键的作用。我们还证明，玉米和水稻中的贮藏蛋白导致较弱的弹性，这表明小麦面筋具有独特的特性。
