Data

Comparative proteomics study of the conglutin proteins across 46 narrow-leafed lupin accessions

Commonwealth Scientific and Industrial Research Organisation
Tahmasian, Arineh ; Colgrave, Michelle ; Broadbent, James ; JUHASZ, Angela ; Nye-Wood, Mitchell
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=info:doi10.25919/pfkr-s130&rft.title=Comparative proteomics study of the conglutin proteins across 46 narrow-leafed lupin accessions&rft.identifier=https://doi.org/10.25919/pfkr-s130&rft.publisher=Commonwealth Scientific and Industrial Research Organisation&rft.description=The most abundant proteins in lupin seeds are the conglutin proteins which are classified into four major families: α, β, γ and δ. These seed storage proteins, play a major role in supplying nitrogen, carbon, and sulphur to the growing seedling during germination and contribute to specific pharmaceutical and nutritional attributes. For instance, the beta conglutin proteins with desirable techno-functional characteristics are known as the main allergenic proteins in lupin seed, whilst the gamma conglutin proteins have been reported to possess strong anti-diabetic properties. Herein, a combination of discovery and targeted quantitative proteomics approaches were used for evaluating the diversity of the conglutin profiles across 46 genetically diverse narrow-leafed lupin (NLL, Lupinus angustifolius) accessions. This collection includes the following data:\n1- The information-dependent acquisition mass spectrometry (IDA-MS) data \n2- ProteinPilot Reports for the IDA data which includes information about the data quality and protein and peptide identifications\n3-Multiple reaction monitoring-mass spectrometry (LC-MRM-MS) data \nLineage: The discovery-based data for this study was acquired on a TripleTOF 6600 MS (SCIEX) and searched against a lupin specific protein database using the ProteinPilot 5.0.3 software (SCIEX), whilst MRM data acquisition was conducted on a 6500+ QTRAP MS (SCIEX).&rft.creator=Tahmasian, Arineh &rft.creator=Colgrave, Michelle &rft.creator=Broadbent, James &rft.creator=JUHASZ, Angela &rft.creator=Nye-Wood, Mitchell &rft.date=2021&rft.edition=v1&rft_rights=Creative Commons Attribution 4.0 International Licence https://creativecommons.org/licenses/by/4.0/&rft_rights=Data is accessible online and may be reused in accordance with licence conditions&rft_rights=All Rights (including copyright) CSIRO, Edith Cowan University 2021.&rft_subject=Lupin&rft_subject=Narrow-leafed lupin&rft_subject=Plant-based protein&rft_subject=Conglutin&rft_subject=Lupinus angustifolius&rft_subject=Proteomics&rft_subject=LC-MS&rft_subject=Proteins and peptides&rft_subject=Medicinal and biomolecular chemistry&rft_subject=CHEMICAL SCIENCES&rft.type=dataset&rft.language=English Access the data

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Creative Commons Attribution 4.0 International Licence
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Data is accessible online and may be reused in accordance with licence conditions

All Rights (including copyright) CSIRO, Edith Cowan University 2021.

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Brief description

The most abundant proteins in lupin seeds are the conglutin proteins which are classified into four major families: α, β, γ and δ. These seed storage proteins, play a major role in supplying nitrogen, carbon, and sulphur to the growing seedling during germination and contribute to specific pharmaceutical and nutritional attributes. For instance, the beta conglutin proteins with desirable techno-functional characteristics are known as the main allergenic proteins in lupin seed, whilst the gamma conglutin proteins have been reported to possess strong anti-diabetic properties. Herein, a combination of discovery and targeted quantitative proteomics approaches were used for evaluating the diversity of the conglutin profiles across 46 genetically diverse narrow-leafed lupin (NLL, Lupinus angustifolius) accessions. This collection includes the following data:
1- The information-dependent acquisition mass spectrometry (IDA-MS) data
2- ProteinPilot Reports for the IDA data which includes information about the data quality and protein and peptide identifications
3-Multiple reaction monitoring-mass spectrometry (LC-MRM-MS) data
Lineage: The discovery-based data for this study was acquired on a TripleTOF 6600 MS (SCIEX) and searched against a lupin specific protein database using the ProteinPilot 5.0.3 software (SCIEX), whilst MRM data acquisition was conducted on a 6500+ QTRAP MS (SCIEX).

Available: 2021-12-23

Data time period: 2020-07-01 to 2020-11-30

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