High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498449210  61 QPEPVSPKPVANHTQGPGQGtnisnsQGPIQGGVPTRPSQAEGAVQGGDSREHVQGGDSRRPGQDRNSVKPGQAEVPFQA 140
Cdd:pfam03157 519 QPGQGQPGYYPTSPQQPGQG------QQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQG 592

                  ..
gi 1498449210 141 TP 142
Cdd:pfam03157 593 QP 594

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498449210  61 QPEPVSPKPVANHTQGPGQGtnisnsQGPIQGGVPTRPSQAEGAVQGGDSREHVQGGDSRRPGQDRNSVKPGQAEVPFQA 140
Cdd:pfam03157 519 QPGQGQPGYYPTSPQQPGQG------QQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQG 592

                  ..
gi 1498449210 141 TP 142
Cdd:pfam03157 593 QP 594

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498449210  61 QPEPVSPKPVANHTQGPGQGtnisnsQGPIQGGVPTRPSQAEGAVQGGDSREHVQGGDSRRPGQDRNSVKPGQAEVPFQA 140
Cdd:pfam03157 519 QPGQGQPGYYPTSPQQPGQG------QQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQG 592

                  ..
gi 1498449210 141 TP 142
Cdd:pfam03157 593 QP 594