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Analysis of peptides formed by an extended semisynthetic protease nanomachine

ABSTRACT: Within the cell, chemical reactions are often confined and organized through a modular architecture. In this project, a cell-free nanoscale model was analyzed that exploits this compartmentalization principle to perform regulated protein unfolding and degradation. To this end, protein degradation products resulting from degradation by the protease chymotrypsin, which was encapsulated in a DNA nanocompartment, were identified and quantified using an LFQ algorithm.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Farnusch Kaschani

LAB HEAD: Farnusch Kaschani

PROVIDER: PXD045825 | Pride | 2024-07-25

REPOSITORIES: Pride

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			Action	DRS
	ACE_0761-01_Search_PD04.7z	Other
	ACE_0761_02.fasta	Fasta
	ACE_0761_JH01.raw	Raw
	ACE_0761_JH02.raw	Raw
	ACE_0761_JH03.raw	Raw

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Modular DNA origami compartments for the engineering of a protein unfolding and degradation pathway

Project description:Within the cell, chemical reactions are often confined and organized through a modular architecture. In this project, a cell-free nanoscale model of the proteasome was analyzed that exploits this compartmentalization principle to perform regulated protein unfolding and degradation. To this end, the protein unfolding machine p97 and the protease chymotrypsin were encapsulated in different DNA nanocompartments, and the sequential unfolding and proteolytic degradation of a model substrate, I3mEos were monitored at different time points via LC-MS/MS-based proteomics using LFQ quantification.

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