MOLECULAR MODELING OF TWO HEXAPEPTIDE REPEAT MOTIFS OF HMW GLUTENIN SUBUNITS

2001 ◽  
Vol 12 (02) ◽  
pp. 281-292 ◽  
Author(s):  
HANDAN ARKIN ◽  
FATİH YAŞAR ◽  
TARIK ÇELİK ◽  
SÜEDA ÇELİK ◽  
HAMİT KÖKSEL
Keyword(s):  
Three Dimensional ◽  
Glutenin Subunits ◽  
Central Domain ◽  
Hmw Glutenin Subunits ◽  
Simulation Procedure ◽  
Helical State ◽  
Letter Code ◽  
Hmw Glutenin ◽  
High Level ◽  
Ramachandran Plots

The three-dimensional structures of two hexapeptide repeat motifs (PGQGQQ and SGQGQQ, in one letter code) in the repetitive central domain of HMW glutenin subunits are investigated by using the multicanonical simulation procedure. Ramachandran plots were prepared and analyzed to predict the relative occurrence probabilities of β-turn and γ-turn structures and helical state. Structural predictions of PGQGQQ repeat motif indicated the presence of high level of β-turns and considerable level of γ-turns. Simulations of the repeat motifs in the repetitive central domain of HMW glutenin subunits indicated that these structures take important part in the three-dimensional structures of repeat motifs.

MULTICANONICAL SIMULATIONS OF FIVE TETRAPEPTIDE SEQUENCES IN THE CENTRAL DOMAIN OF HMW GLUTENIN

2000 ◽  
Vol 11 (08) ◽  
pp. 1595-1606 ◽  
Author(s):  
HANDAN ARKIN ◽  
FATİH YAŞAR ◽  
TARIK ÇELİK ◽  
SÜEDA ÇELİK ◽  
HAMİT KÖKSEL
Keyword(s):  
Three Dimensional ◽  
Simulation Method ◽  
Glutenin Subunits ◽  
Central Domain ◽  
Small Proteins ◽  
Letter Code ◽  
Hmw Glutenin ◽  
High Level ◽  
Ramachandran Plots ◽  
Proteins And Peptides

The application of the multicanonical simulation method to small proteins and peptides seems to be feasible and should be undertaken. In this work, the three-dimensional structures of five common tetrapeptide sequences (QPGQ, QSGQ, YPTS, SPQQ and QPGY, in one letter code) in the repetitive central domain of HMW glutenin subunits are investigated by using the multicanonical simulation procedure. Ramachandran plots were prepared and analyzed to predict the relative occurrence probabilities of β-turn and γ-turn structures and helical states. Structural predictions of the five tetrapeptide sequences indicated the presence of high level of β-turns and considerable level of γ-turns. It was also possible to distinguish different type of turns and their occurrence probabilities.

STUDY OF TWO BIOACTIVE PEPTIDES IN VACUUM AND SOLVENT BY MOLECULAR MODELING

2006 ◽  
Vol 17 (06) ◽  
pp. 825-839
Author(s):  
F. YAŞAR ◽  
K. DEMIR
Keyword(s):  
Molecular Modeling ◽  
Three Dimensional ◽  
Helical Structures ◽  
Surface Areas ◽  
Solvent Model ◽  
Letter Code ◽  
End Distance ◽  
Accessible Surface ◽  
High Level ◽  
Ramachandran Plots

The thermodynamic and structural properties of Tyrosine-Glycine-Leusine-Phenylalanine (YGLF, in a one letter code) and Lysine-Valine-Leusine-Proline-Valine-Proline-Glutamine (KVLPVPQ) peptide sequences were studied by three-dimensional molecular modeling in vacuum and solution. All the three-dimensional conformations of each peptide sequences were obtained by multicanonical simulations with using ECEPP/2 force field and each simulation started from completely random initial conformation. Solvation contributions are included by a term that is proportional to solvent-accessible surface areas of peptides. In the present study, we calculated the average values of total energy, specific heat, fourth-order cumulant and end-to-end distance for two peptide sequences of milk protein as a function of temperature. With using major advantage of this simulation technique, Ramachandran plots were prepared and analysed to predict the relative occurrence probabilities of β-turn, γ-turn and helical structures. Although structural predictions of these sequences indicate both the presence of high level of γ-turns and low level of β-turns in vacuum and solvent, it was observed that these probabilities in vacuum were higher than the ones in solvent model.

Transfer of HMW-glutenin subunits from wild wheats into Triticum durum and improvement of quality

2002 ◽  
Vol 30 (1-2) ◽  
pp. 173-180 ◽  
Author(s):  
H. S. Dhaliwal ◽  
M. Garg ◽  
H. Singh ◽  
P. Chhuneja ◽  
Harinder Kaur
Keyword(s):  
Triticum Durum ◽  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Wild Wheats ◽  
Hmw Glutenin

Composition of and variation in high- and low-molecular weight glutenin subunits, and omega gliadins in Ethiopian tetraploid wheat germplasm

2006 ◽  
Vol 4 (2) ◽  
pp. 134-143 ◽  
Author(s):  
Faris Hailu ◽  
Eva Johansson ◽  
Arnulf Merker ◽  
Getachew Belay ◽  
Harjit-Singh ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Tetraploid Wheat ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Lmw Glutenin Subunits ◽  
Hmw Glutenin ◽  
Omega Gliadins ◽  
High Degree

A collection of 120 Ethiopian tetraploid wheat accessions was analysed for high-molecular weight (HMW) glutenin subunit, low-molecular weight (LMW) glutenin subunit and omega gliadin composition by SDS–PAGE. For the HMW glutenin subunits, a new allelic variant, 2****, was detected which has not been previously described at the Glu-A1 locus. A high proportion of Glu-A1x banding pattern was observed in durum wheat. For the Glu-B1 locus four different banding patterns were detected. Among those HMW glutenin subunits, 7+8 were the most common, while subunits 14+15 and 6+8 were found to be rare. A high degree of variation was evident for the LMW glutenin subunits and D-zone omega gliadins. The association of the composition of the gluten with quality has been discussed. This wide variation can be used in improving the quality of wheat and to widen its genetic base.

scholarly journals Pyramiding of Genes for Grain Protein Content, Grain Quality and Rust Resistance in Eleven Indian Bread Wheat Cultivars: A Multi-Institutional Effort

2021 ◽  
Author(s):  
Pushpendra K. Gupta ◽  
Harindra S. Balyan ◽  
Parveen Chhuneja ◽  
Jai P. Jaiswal ◽  
Shubhada Tamhankar ◽  
...  
Keyword(s):  
Protein Content ◽  
Rust Resistance ◽  
Grain Quality ◽  
Grain Protein Content ◽  
Grain Protein ◽  
Loaf Volume ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Hmw Glutenin

Abstract Improvement of grain protein content (GPC), loaf volume and resistance to rusts was achieved in 11 Indian wheat cultivars that are widely grown in four different agro-climatic zones of India. This involved use of marker-assisted backcrossing (MABC) for introgression and pyramiding of the following genes: (i) the high GPC gene Gpc-B1; (ii) HMW glutenin subunits 5 + 10 at Glu-D1 loci, and (iii) rust resistance genes, Yr36, Yr15, Lr24 and Sr24. GPC was improved by 0.8–3.3%, although high GPC was generally associated with yield penalty. Further selection among high GPC lines, allowed development of progenies with higher GPC associated with improvement in 1000-grain weight and grain yield in the following four cultivars: NI5439, UP2338, UP2382 and HUW468. The high GPC progenies (derived from NI5439) were also improved for grain quality using HMW glutenin subunits 5 + 10 at Glu-D1 loci. Similarly, progenies combining high GPC and rust resistance were developed in the backgrounds of following five cultivars: Lok1, HD2967, PBW550, PBW621 and DBW1. The improved pre-bred lines developed during the present study should prove useful for development of cultivars with improved nutritional quality associated with rust resistance in future wheat breeding programmes.

Quality Influence Comparison of Some x- and y-Type HMW Glutenin Subunits Coded by Glu-D1 Locus

2001 ◽  
pp. 189-194
Author(s):  
M. Rodríguez-Quijano ◽  
M. T. Nieto-Taladriz ◽  
M. Gómez ◽  
J. F. Vázquez ◽  
J. M. Carrillo
Keyword(s):  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Hmw Glutenin

scholarly journals Variation in HMW glutenin subunits of different species of wheat

2011 ◽  
Vol 48 (No. 1) ◽  
pp. 15-19
Author(s):  
Z. Gálová ◽  
MichalíkI ◽  
H. Knoblochová ◽  
E. Gregová
Keyword(s):  
Triticum Turgidum ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Varieties ◽  
Hmw Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin ◽  
Triticum Durum Desf

Method ISTA SDS-PAGE was used for separation, detection and evaluation of high molecular weight glutenin subunits (HMW) in the different wheat species. The relation has been studied between the HMW glutenin subunit alleles and the bread-making quality of 25 world wheat cultivars and 21 regional varieties common wheat varieties (Triticum aestivum L.), 17 winter spelt wheat (Triticum spelta L.), 3 durum wheat cultivars (Triticum durum DESF.), 9 cultivars of Triticum turgidum L. and 5 cultivars of Triticum polonicum L. The highest frequency of occurrence of HMW glutenin subunits 2*, 13 + 16 and 5 + 10 were found in world wheat cultivars. In Slovak wheat varieties were analysed subunits 0, 7 + 9 and 5 + 10, 2 + 12. The HMW subunits 0, 7 + 8 with Glu-score 4 were determined in Triticum durum DESF. Three electrophoretical profile groups of different HMW glutenin subunits were found in Triticum turgidum L. and Triticum polonicum L. and six electrophoretical profile groups were determined in Triticum spelta L. The verified correlations between bread-making quality and specific HMW subunits of glutenin can be utilised by wheat breeders using SDS-PAGE of proteins as a screening test for the prediction of bread-making quality of wheat.

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