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UnknownData-independent Acquisition Improves Quantitative Cross-linking Mass Spectrometry.
Not available
S-EPMC6442367 | biostudies-literature
ProteomicsQuantitative photo-crosslinking mass spectrometry reveals protein structure response to environmental changes
Conformational changes of protein structures depend on their chemical and physical environment. Studying conformational changes depending on environmental parameters is notoriously difficult as many methods of structural biology are affected by parameters like temperature or pH. To make such conform...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2019-07-01 | PXD012939 | Pride
Data-independent acquisition Structural dynamics Human serum albumin Dia-qclms Quantitation Xi Cytochrome c Spectronaut Label-free Mass spectrometry Photo-crosslinking Cross-linking Sda 
UnknownQuantitative Photo-crosslinking Mass Spectrometry Revealing Protein Structure Response to Environmental Changes.
Not available
S-EPMC6639777 | biostudies-literature
ProteomicsData independent acquisition cross-linking/mass spectrometry
Quantitative cross-linking/mass spectrometry (QCLMS) provides increasing structural detail on altered protein states in solution. Accurate quantitation is a value in itself but may also be central to elucidating small differences between protein states. Hence, QCLMS could benefit from data independe...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) Gallus gallus (Chicken) Equus caballus (Horse) 
2019-01-25 | PXD011036 | Pride
Xi Reproducibility Spectronaut Data independent acquisition Label-free Mass spectrometry Quantitation Cross-linking 
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