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PXD054603

PXD054603 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleRevisiting the effect of trypsin digestion buffers on artificial deamidation
DescriptionDeamidation of asparagine and glutamine residues occurs spontaneously, accelerated by adjacent amino acid residues and influenced by pH, temperature, and incubation time. Standard proteolytic digestion induces significant deamidation, which is especially problematic in bottom-up proteomic studies. Trypsin digestion protocol modifications, including shorter incubation times and specific lysis buffers are shown to minimize deamidation. Herein, HEPES is proven to be most optimal due to reduced deamidation coupled with its compatibility for both proteins and trypsin digestion, highlighting its suitability for maintaining sample integrity in biological research contexts.
HostingRepositoryPRIDE
AnnounceDate2025-03-11
AnnouncementXMLSubmission_2025-03-11_07:14:58.991.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterEmmajay Sutherland
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationListmonohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Ascend
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-08-05 09:22:14ID requested
12025-03-11 07:14:59announced
Publication List
10.1021/jasms.4c00389;
Sutherland E, Veth TS, Riley NM, Revisiting the Effect of Trypsin Digestion Buffers on Artificial Deamidation. J Am Soc Mass Spectrom, 36(3):457-462(2025) [pubmed]
Keyword List
submitter keyword: de-glycopeptides,Chemical deamidation, de-glycoproteomics
Contact List
Nicholas M. Riley
contact affiliationDepartment of Chemistry University of Washington, Seattle, WA, USA
contact emailnmriley@uw.edu
lab head
Emmajay Sutherland
contact affiliationUniversity of Washington
contact emailemmajay.sutherland@gmail.com
dataset submitter
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Dataset FTP location
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