Data for: Quantitative LC-MS intact proteoform profiling of reduced wheat gluten

Intact proteoform profiling of glutenin fractions from two Canadian breadwheat varieties and 28 F5 crosses. Masses range from 18-88 kDa were deconvolved using MaxEnt1 deconvolution from non-monoisotopically resolved data. Proteoform abundances were expressed as MaxEnt1 peak areas using a custom algorithm. Proteoforms were grouped within samples (WSG) to eliminate artifacts and proteoforms occurring in adjacent deconvolution windows. A similar grouping algorithm (ASG) was used to provide common proteoform numbers (ASG numbers) across each sample set. Control sample data from each set were extracted and compared pair-wise to a common set (set 1) to obtain linear regression coefficients to correct retention time and abundance shifts between sample sets (CHKNorm procedure). These coefficients were then used to correct sample set data to render them comparable. Proteoform abundances were not retained unless detected in both replicates for that sample.A 20% RSD threshold (replicate abundances) was calculated from replicate variability across the data set and candidate proteoforms not present in at least one sample above this threshold (4.3 million counts) were eliminated from the final dataset

Elucidation of High-molecular weight glutenin C-terminal truncation

MS-MS data supporting the identification of C-terminal truncation of Dy and Bx high-molecular weight glutenin subunits (HMWGS) in wheat. HMWGS Dy10 and Bx7* were purified from the Canadian bread wheat variety Carberry. Refer to manuscript for details (see Related Links, below).Data were acquired on a Waters G2 Synapt in MS-MS mode.File index:Direct infusion of peptide standards (Dy10 intact, Dy10 truncated, Bx7* Intact, Bx7* truncated). Acquisitions in MS-MS mode with CE (trap) switched on halfway through run:FileDescription20230417 DY10 IN MS_02.rawm/z = 1282.615, CE = 6520230417 DY10 IN MS_03.rawm/z = 855.413, CE = 3120230417 DY10 IN MS_04.rawm/z = 641.811, CE = 17 (Moved CE around in last 10 scans)20230417 DY10 TR MS_02.rawm/z = 1003.975, CE = 6020230417 DY10 TR MS_03.rawm/z = 669.652, CE = 2520230417 INF BX7S IN MS-MS_01.rawm/z = 1332.173, CE = 8020230417 INF BX7S IN MS-MS_02.rawm/z = 1332.173, CE = 8520230417 INF BX7S IN MS-MS_03.rawm/z = 888.451, CE = 3720230417 INF BX7S IN MS-MS_04.rawm/z = 888.451, CE = 3020230417 INF BX7S TR MS_02.rawm/z = 1003.993, CE = 4720230417 INF BX7S TR MS_03.rawm/z = 669.664, CE = 2520230417 LEUENK_01.rawMS1 only, LeuEnk for mass correctionLC-MS-MS of sample digests using CE as optimized above:FileDescription20230420 Dig_Bx7s_HDms-ms_01.rawBx7* digest (rLysC)20230420 Dig_Dy10_HDms-ms_01.rawDy10 digest (rLysC)20230420 PEP_Bx7s_I_HDms-ms_01.rawBx7* intact standard peptide20230420 PEP_Bx7s_T_HDms-ms_01.rawBx7* truncated standard peptide20230420 PEP_Dy10_I_HDms-ms_01.rawDy10 intact standard peptide20230420 PEP_Dy10_T_HDms-ms_01.rawDy10 truncated standard peptideAll samples pyridylethylated prior to analysis

Data for: Quantitative LC-MS intact proteoform profiling of reduced wheat gluten

Intact proteoform profiling of glutenin fractions from two Canadian breadwheat varieties and 28 F5 crosses. Masses range from 18-88 kDa were deconvolved using MaxEnt1 deconvolution from non-monoisotopically resolved data. Proteoform abundances were expressed as MaxEnt1 peak areas using a custom algorithm. Proteoforms were grouped within samples (WSG) to eliminate artifacts and proteoforms occurring in adjacent deconvolution windows. A similar grouping algorithm (ASG) was used to provide common proteoform numbers (ASG numbers) across each sample set. Control sample data from each set were extracted and compared pair-wise to a common set (set 1) to obtain linear regression coefficients to correct retention time and abundance shifts between sample sets (CHKNorm procedure). These coefficients were then used to correct sample set data to render them comparable. Proteoform abundances were not retained unless detected in both replicates for that sample.A 20% RSD threshold (replicate abundances) was calculated from replicate variability across the data set and candidate proteoforms not present in at least one sample above this threshold (4.3 million counts) were eliminated from the final dataset.THIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV

Data for: Quantitative LC-MS intact proteoform profiling of reduced wheat gluten

Intact proteoform profiling of glutenin fractions from two Canadian breadwheat varieties and 28 F5 crosses. Masses range from 18-88 kDa were deconvolved using MaxEnt1 deconvolution from non-monoisotopically resolved data. Proteoform abundances were expressed as MaxEnt1 peak areas using a custom algorithm. Proteoforms were grouped within samples (WSG) to eliminate artifacts and proteoforms occurring in adjacent deconvolution windows. A similar grouping algorithm (ASG) was used to provide common proteoform numbers (ASG numbers) across each sample set. Control sample data from each set were extracted and compared pair-wise to a common set (set 1) to obtain linear regression coefficients to correct retention time and abundance shifts between sample sets (CHKNorm procedure). These coefficients were then used to correct sample set data to render them comparable. Proteoform abundances were not retained unless detected in both replicates for that sample.A 20% RSD threshold (replicate abundances) was calculated from replicate variability across the data set and candidate proteoforms not present in at least one sample above this threshold (4.3 million counts) were eliminated from the final dataset.THIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV

Elucidation of High-molecular weight glutenin C-terminal truncation

MS-MS data supporting the identification of C-terminal truncation of Dy and Bx high-molecular weight glutenin subunits (HMWGS) in wheat. HMWGS Dy10 and Bx7* were purified from the Canadian bread wheat variety Carberry. Refer to manuscript for details (see Related Links, below).Data were acquired on a Waters G2 Synapt in MS-MS mode.File index:Direct infusion of peptide standards (Dy10 intact, Dy10 truncated, Bx7* Intact, Bx7* truncated). Acquisitions in MS-MS mode with CE (trap) switched on halfway through run:FileDescription20230417 DY10 IN MS_02.rawm/z = 1282.615, CE = 6520230417 DY10 IN MS_03.rawm/z = 855.413, CE = 3120230417 DY10 IN MS_04.rawm/z = 641.811, CE = 17 (Moved CE around in last 10 scans)20230417 DY10 TR MS_02.rawm/z = 1003.975, CE = 6020230417 DY10 TR MS_03.rawm/z = 669.652, CE = 2520230417 INF BX7S IN MS-MS_01.rawm/z = 1332.173, CE = 8020230417 INF BX7S IN MS-MS_02.rawm/z = 1332.173, CE = 8520230417 INF BX7S IN MS-MS_03.rawm/z = 888.451, CE = 3720230417 INF BX7S IN MS-MS_04.rawm/z = 888.451, CE = 3020230417 INF BX7S TR MS_02.rawm/z = 1003.993, CE = 4720230417 INF BX7S TR MS_03.rawm/z = 669.664, CE = 2520230417 LEUENK_01.rawMS1 only, LeuEnk for mass correctionLC-MS-MS of sample digests using CE as optimized above:FileDescription20230420 Dig_Bx7s_HDms-ms_01.rawBx7* digest (rLysC)20230420 Dig_Dy10_HDms-ms_01.rawDy10 digest (rLysC)20230420 PEP_Bx7s_I_HDms-ms_01.rawBx7* intact standard peptide20230420 PEP_Bx7s_T_HDms-ms_01.rawBx7* truncated standard peptide20230420 PEP_Dy10_I_HDms-ms_01.rawDy10 intact standard peptide20230420 PEP_Dy10_T_HDms-ms_01.rawDy10 truncated standard peptideAll samples pyridylethylated prior to analysis.THIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV

Fusarium protease reduction of gluten strength

Development of fluorescence assay for Fusarium protease damage to gluten, Extensigraph Rmax characterization of blends of Fusarium damaged seed into sound base, Fusarium protease analysis of single infected seeds and digestion of bovine beta casein using sound and Fusarium damaged seed extracts as enzyme source. Data shows increase in protease with infected seed content and reduction in Extensigraph Rmax (indicator of gluten strength). Digestion of beta-casein indicates preference for K at P1 position, isoleucine at P1 and P1', arginine at P1' and tyrosine at P1.THIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV