Proteomics

Dataset Information

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Protein Structure Determination in Biological Matrices by Mass Spectrometry and Computational Biology


ABSTRACT: We have implemented the use of a heterobifunctional, UV photoactivatable cross-linker, which greatly increases the number of identified cross-links compared with homobifunctional, NHS-ester based cross-linkers. We have cross-linked human serum albumin in the context of human blood serum. We present a novel methodology that combines the use of this high-resolution cross-linking with conformational space search to investigate the structure of proteins in their native environment.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

SUBMITTER: Adam Belsom  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD001692 | Pride | 2015-09-22

REPOSITORIES: Pride

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Publications

Serum Albumin Domain Structures in Human Blood Serum by Mass Spectrometry and Computational Biology.

Belsom Adam A   Schneider Michael M   Fischer Lutz L   Brock Oliver O   Rappsilber Juri J  

Molecular & cellular proteomics : MCP 20150918 3


Chemical cross-linking combined with mass spectrometry has proven useful for studying protein-protein interactions and protein structure, however the low density of cross-link data has so far precluded its use in determining structures de novo. Cross-linking density has been typically limited by the chemical selectivity of the standard cross-linking reagents that are commonly used for protein cross-linking. We have implemented the use of a heterobifunctional cross-linking reagent, sulfosuccinimi  ...[more]

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