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aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds. The way the glutenins form their disulfide bond network is predicted to be regulated by the hydrophobicity in the peptide sections where their cysteins are located, explaining why the gliadins are
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Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits. It has been demonstrated that alleles Glu-A1b (Ax2∗) and Glu-D1d (Dx5 + Dy10) are normally associated with superior end-use quality, especially dough strength.
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proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins. They are structurally similar to LMW glutenins. Glutenins occur as
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341:"Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations"
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monomeric despite sharing similar conserved cysteine motifs as the LMW-glutenins.
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and other forces. Glutenin is responsible for the strength and elasticity of
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from about 200,000 to a few million, which are stabilized by intermolecular
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proteins consist of two major fractions: the gliadins and the glutenins.
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Markgren J, Hedenqvist M, Rasheed F, Skepö M, Johansson E (July 2020).
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109:Learn how and when to remove this message
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47:adding citations to reliable sources
249:(HMW) and low-molecular-mass (LMW)
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392:family:"gliadin glutenin family"
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170:Available protein structures:
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263:hydrophobic interactions
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41:Please help
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351:(8): 1095.
243:wheat flour
233:(a type of
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286:multimeric
182:structures
69:newspapers
58:"Glutenin"
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282:monomeric
160:IPR001419
99:June 2017
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316:Springer
278:Gliadins
251:subunits
235:glutelin
231:Glutenin
199:RCSB PDB
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137:Glutenin
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408:Gluten
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