PXD007994 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Reversible Lysine Derivatization Enables High Specificity of Arg-C Digestion Using Trypsin |
Description | Bottom-up proteomics approach has become an important strategy in diverse areas of biological research, and the enzymatic digestion is essential for this technology. Endopeptidase Arg-C catalyzing the hydrolytic cleavage of peptide bonds C-terminal to arginine could be an important protease in bottom-up proteomics. However, it has been seldom applied due to its low specificity and high cost. Reversible chemical derivatization of amine allows a real Arg-C digestion using trypsin. In this paper, a reversible amine derivatization method, citraconylation and decitraconylation were optimized and evaluated for large-scale proteomics studies. Combination of the reversible derivatization and trypsin digestion (termed Arg-C* digestion to distinguish from the conventional Arg-C digestion) resulted in 64.2% more peptide identification (11,925 ± 199 vs 7,262 ± 59) and significantly higher cleavage specificity (95.6% vs 73.6%) than the conventional Arg-C digestion. Comparison of Arg-C* digestion with the widely used trypsin and Lys-C digestion revealed that Arg-C* performed equally or slightly better than Lys-C although not comparable to trypsin. Therefore, the well-established Arg-C* digestion method is a promising approach for proteomics studies and could be used as the prior alternative digestion method to trypsin digestion in order to achieve higher proteome coverage. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:16:25.350.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Zhen Wu |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | S-carboxamidoethyl-L-cysteine; monohydroxylated residue |
Instrument | LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-10-18 07:03:56 | ID requested | |
1 | 2018-01-04 03:02:50 | announced | |
⏵ 2 | 2024-10-22 04:16:26 | announced | 2024-10-22: Updated project metadata. |
Publication List
Keyword List
curator keyword: Technical |
submitter keyword: proteomics, Arg-C, trypsin, Lys-C,citraconylation, LC-MS/MS |
Contact List
Xumin Zhang |
contact affiliation | State Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai 200438, China |
contact email | xumin_zhang@fudan.edu.cn |
lab head | |
Zhen Wu |
contact affiliation | State Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University |
contact email | wuz16@fudan.edu.cn |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2018/01/PXD007994 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD007994
- Label: PRIDE project
- Name: Reversible Lysine Derivatization Enables High Specificity of Arg-C Digestion Using Trypsin