MassIVE MSV000092130

Partial Public PXD042825

Native Nanoproteomics Captures Structure and Dynamics of Endogenous Protein Complexes in Human Heart Tissue

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Description

To obtain a molecular-level understanding of biological processes, it is critical to perform structural characterization of protein complexes and their subunits directly from human tissues. Native top-down mass spectrometry (MS) has emerged as a complementary technique to traditional structural biology methods. Nonetheless, native top-down MS has primarily characterized recombinant or high-abundance protein complexes, as strategies to enrich and preserve low-abundance protein complexes from human tissues is lacking. Here we have developed a native nanoproteomics platform integrating peptide-functionalized nanoparticles to characterize low-abundance protein complexes with high-resolution native top-down MS. We then apply our native nanoproteomics strategy to enrich and structurally elucidate endogenous troponin (cTn) complexes directly from human heart tissue. Our results not only reveal the native complex assembly, post-translational modification landscape, and Ca2+ binding dynamics of the cTn complex but also enable us to propose a paradigm for structural and dynamical characterization of endogenous native protein complexes from human tissues. [doi:10.25345/C56970784] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Native top-down ; Mass spectrometry ; Endogenous protein complex ; cardiac troponin ; nanoproteomics

Contact

Principal Investigators:
(in alphabetical order) 		Ying Ge, University of Wisconsin - Madison, United States of America
Submitting User: eachapman2
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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