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The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants

ABSTRACT: 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.

INSTRUMENT(S):

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

SUBMITTER: Michael Kreutzer

LAB HEAD: Michael O.

PROVIDER: PXD064233 | Pride | 2025-11-28

REPOSITORIES: Pride

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			Action	DRS
	DB_PCR_pep_20221117.fasta	Fasta
	F417287.dat	Other
	F417287.mgf	Mgf
	FOLDON_0_01a.raw.zip	Raw
	FOLDON_0_02a.raw.zip	Raw

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