Proteomics

Dataset Information

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Evaluation of NHS-Acetate and DEPC labelling for determination of solvent accessible amino acid residues in protein complexes


ABSTRACT: The structural analysis of proteins and protein complexes is key for understanding their function and regulation. In order to gain structural information, we examined protein surface labelling using NHS-Acetate and DEPC following an MS-based workflow. Using two model proteins we characterise the obtained mass spectra and explore the applicability of a quantitative approach for determining of solvent accessible amino acid residues on the surface of proteins and protein complexes. The modified peptides were analysed by LC-MS/MS and processed using MaxQuant for identification and intensity determination of labelled and unlabelled peptides.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Oryctolagus Cuniculus Cuniculus Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Marie Alfes  

LAB HEAD: Carla Schmidt

PROVIDER: PXD015940 | Pride | 2020-05-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ADH_DEPC_0_0_mM_R1.raw Raw
ADH_DEPC_0_0_mM_R2.raw Raw
ADH_DEPC_0_0_mM_R3.raw Raw
ADH_DEPC_0_1_mM_R1.raw Raw
ADH_DEPC_0_1_mM_R2.raw Raw
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Publications

Evaluation of NHS-Acetate and DEPC labelling for determination of solvent accessible amino acid residues in protein complexes.

Barth Marie M   Bender Julian J   Kundlacz Til T   Schmidt Carla C  

Journal of proteomics 20200427


The activity of most proteins and protein complexes relies on the formation of defined three-dimensional structures. The analysis of these arrangements is therefore key for understanding their function and regulation in the cell. Besides the traditional structural techniques, structural mass spectrometry delivers insights into the various aspects of protein structure, including stoichiometry, protein-ligand interactions and solvent accessibility. The latter is usually obtained from labelling exp  ...[more]

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