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Intact Transition Epitope Mapping - Forces of Interactions between Variants of Equivalent macromolecules (ITEM-FIVE)

ABSTRACT: Foldon (F) is a specific partial sequence from the C-terminal domain of T4 fibritin, which is found at the neck of the T4 bacteriophage. The amino acid sequence (27 residues) in single letter code is GYIPEAPRDGQAYVRKDGEWVLLSTFL. In neutral solution (pH 6.9) it forms a homo-trimer (F-F-F). Biotinylated foldon (bF) is composed of the exact same amino acid sequence but contains a biotin residue attached to the N-terminal amino acid residue via two PEG linker molecules. In solution with neutral pH it forms a homo-trimer (bF-bF-bF). Mixing of both homo-trimers in solution with neutral pH spontaneously produces hetero-trimers (F-F-bF and F-bF-bF).

INSTRUMENT(S): Synapt MS

ORGANISM(S): Enterobacteria Phage T4 (bacteriophage T4)

SUBMITTER: Michael Kreutzer

LAB HEAD: Prof. Dr. Michael O. Glocker

PROVIDER: PXD044721 | Pride | 2024-04-29

REPOSITORIES: Pride

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Intact Transition Epitope Mapping-Force Interferences by Variable Extensions (ITEM-FIVE).

Koy Cornelia C Röwer Claudia C Thiesen Hans-Jürgen HJ Neamtu Andrei A Glocker Michael O MO

Biomolecules 20240408 4

Investigations on binding strength differences of non-covalent protein complex components were performed by mass spectrometry. T4 fibritin foldon (T4Ff) is a well-studied miniprotein, which together with its biotinylated version served as model system to represent a compactly folded protein to which an Intrinsically Disordered Region (IDR) was attached. The apparent enthalpies of the gas phase dissociation reactions of the homo-trimeric foldon F-F-F and of the homo-trimeric triply biotinylated f ...[more]

PMID: 38672470

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