Proteomics

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Chen Minor et al 2023 Mass Spectrometry Data


ABSTRACT: Purified protein complexes were separated by SDS-PAGE and gel lanes divided into 3 sections (A, B and C). Samples prepared in triplicate (1, 2 and 3). A nanoElute (Bruker) was attached in line to a timsTOF Pro equipped with a CaptiveSpray Source (Bruker, Hamburg, Germany). Chromatography was conducted at 40C through a 25cm reversed-phase C18 column (PepSep) at a constant flow-rate of 0.5 uL/min. Mobile phase A was 98/2/0.1% LC/MS grade H2O/ACN/FA (v/v/v) and phase B was LC/MS grade ACN with 0.1% FA (v/v). During a 108 min method, peptides were separated by a 3-step linear gradient (5% to 30% B over 90 min, 30% to 35% B over 10 min, 35% to 95% B over 4 min) followed by a 4 min isocratic flush at 95% for 4 min before washing and a return to low organic conditions. Experiments were run as data-dependent acquisitions with ion mobility activated in PASEF mode. MS and MS/MS spectra were collected with m/z 100 to 1700 and ions with z = +1 were excluded.

INSTRUMENT(S): timsTOF

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Balyn Zaro  

PROVIDER: MSV000090434 | MassIVE |

REPOSITORIES: MassIVE

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Publications

EMC chaperone-Ca<sub>V</sub> structure reveals an ion channel assembly intermediate.

Chen Zhou Z   Mondal Abhisek A   Abderemane-Ali Fayal F   Jang Seil S   Niranjan Sangeeta S   Montaño José L JL   Zaro Balyn W BW   Minor Daniel L DL  

Nature 20230517 7969


Voltage-gated ion channels (VGICs) comprise multiple structural units, the assembly of which is required for function<sup>1,2</sup>. Structural understanding of how VGIC subunits assemble and whether chaperone proteins are required is lacking. High-voltage-activated calcium channels (Ca<sub>V</sub>s)<sup>3,4</sup> are paradigmatic multisubunit VGICs whose function and trafficking are powerfully shaped by interactions between pore-forming Ca<sub>V</sub>1 or Ca<sub>V</sub>2 Ca<sub>V</sub>α<sub>1</  ...[more]

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