In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria

The field of structural biology is increasingly focusing on studying proteins in situ, i.e., in their greater biological context. Cross-linking mass spectrometry (CLMS) is contributing to this effort, typically through the use of mass spectrometry (MS)-cleavable cross-linkers. Here, we apply the pop...

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Vydané v:	Journal of proteome research Ročník 19; číslo 1; s. 327
Hlavní autori:	Ryl, Petra S J, Bohlke-Schneider, Michael, Lenz, Swantje, Fischer, Lutz, Budzinski, Lisa, Stuiver, Marchel, Mendes, Marta M L, Sinn, Ludwig, O'Reilly, Francis J, Rappsilber, Juri
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 03.01.2020
Predmet:	Chromatography, Gel Cross-Linking Reagents - chemistry Humans K562 Cells Mass Spectrometry - methods Mitochondria - chemistry Mitochondrial Proteins - analysis Mitochondrial Proteins - chemistry Protein Conformation Protein Interaction Maps Succinimides - chemistry Workflow noncleavable DSS cross-linker in situ large-scale structural biology comparative modeling human mitochondria cross-linking mass spectrometry
ISSN:	1535-3907, 1535-3907
On-line prístup:	Zistit podrobnosti o prístupe
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