PXD064233 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants |
| Description | The wild-type foldon (foldon 0) is the C-terminal trimerization domain of the bacteriophage T4 Fibritin foldon (T4Ff). T4Ff’s amino acid sequence is GYIPEAPRDGQAYVRKDGEWVLLSTFL (27 amino acid residues; single letter code). Foldons 0, 1-6 were synthesized by solid phase peptide synthesis and in foldons 1-6 D amino acids at positions 10 (G10a) and 17 (D17f) were introduced. In addition, foldons 2-6 carry artificial N-termini consisting of amino acid residues with increasing space-demanding side chains. All foldons, 0-6, form non-covalent trimers in solution and courses of trimer dissociations were investigated after electrospraying supramolecular ions in the gas phase using ITEM-FIVE (Intact Transition Epitope Mapping - Force Interferences by Variable Extensions) mass spectrometry. Differences in trimer stabilities were correlated with structural features. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-11-28 |
| AnnouncementXML | Submission_2025-11-27_22:58:14.669.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Michael Kreutzer |
| SpeciesList | scientific name: Enterobacteria phage T4 (Bacteriophage T4); NCBI TaxID: NEWT:10665; |
| ModificationList | No PTMs are included in the dataset |
| Instrument | Synapt MS |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-05-23 04:20:04 | ID requested | |
| ⏵ 1 | 2025-11-27 22:58:15 | announced | |
Publication List
Keyword List
Contact List
| Michael O. |
| contact affiliation | Director, Proteome Center Rostock, University of Rostock, Germany |
| contact email | michael.glocker@med.uni-rostock.de |
| lab head | |
| Michael Kreutzer |
| contact affiliation | University Medical Center Rostock |
| contact email | michael.kreutzer@med.uni-rostock.de |
| 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/2025/11/PXD064233 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD064233
- Label: PRIDE project
- Name: The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants