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

ABSTRACT: 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, plants take on the often widely ranging temperature of their surroundings, possibly influencing the evolution of protein thermal stability. In this report we present the first in-depth look at the thermal proteome of a plant species, the model organism Arabidopsis thaliana By profiling the melt

SUBMITTER: Volkening JD 

PROVIDER: S-EPMC6356070 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature