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Thermal proteome profiling of Arabidopsis thaliana

ABSTRACT: Six biological replicates of Arabidopsis thaliana were subjected to protein extraction, ten-temperature gradient precipitation, TMT labeling, off-line alkaline fractionation, and LC-MS/MS. The resulting data was used downstream for untargeted modeling of protein unfolding and melting temperature estimation.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Whole Plant

SUBMITTER: Jeremy Volkening

LAB HEAD: Michael R Sussman

PROVIDER: PXD011200 | Pride | 2018-11-23

REPOSITORIES: Pride

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Proteome-wide Analysis of Protein Thermal Stability in the Model Higher Plant <i>Arabidopsis thaliana</i>.

Volkening Jeremy D JD Stecker Kelly E KE Sussman Michael R MR

Molecular & cellular proteomics : MCP 20181106 2

Modern tandem MS-based sequencing technologies allow for the parallel measurement of concentration and covalent modifications for proteins within a complex sample. Recently, this capability has been extended to probe a proteome's three-dimensional structure and conformational state by determining the thermal denaturation profile of thousands of proteins simultaneously. Although many animals and their resident microbes exist under a relatively narrow, regulated physiological temperature range, pl ...[more]

PMID: 30401684

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