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ProteomicsQuantitative cross-linking/mass spectrometry reveals subtle protein conformational changes
We have developed quantitative cross-linking/mass spectrometry (QCLMS) to interrogate conformational rearrangements of proteins in solution. Our workflow was tested using a structurally well-described reference system, the human complement protein C3 and its activated cleavage product C3b. We found ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-06-16 | MSV000079827 | MassIVE
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 
UnknownData-independent Acquisition Improves Quantitative Cross-linking Mass Spectrometry.
Not available
S-EPMC6442367 | biostudies-literature
UnknownQuantitative Photo-crosslinking Mass Spectrometry Revealing Protein Structure Response to Environmental Changes.
Not available
S-EPMC6639777 | biostudies-literature
ProteomicsIsobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes
Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. Here we introduce a nov...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-11-13 | PXD056825 | Pride
Isobaric crosslinkers Qclms Conformational changes Quantitative crosslinking mass spectrometry 
UnknownQuantitative cross-linking/mass spectrometry reveals subtle protein conformational changes.
Not available
S-EPMC5140025 | biostudies-literature
UnknownOn the Reproducibility of Label-Free Quantitative Cross-Linking/Mass Spectrometry.
Not available
S-EPMC5814520 | 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 
ProteomicsOn the reproducibility of label-free quantitative cross-linking/mass spectrometry
Quantitative cross-linking/mass spectrometry (QCLMS) is an emerging approach to study conformational changes of proteins and multi-subunit complexes. Distinguishing protein conformations requires reproducibly identifying and quantifying cross-linked peptides. Here we analyzed the variation between m...
ORGANISM(S): Homo sapiens (Human) 
2018-01-02 | PXD007250 | Pride
Cross-linking Mass-spectrometry Skyline Quatitation 
ProteomicsQuantitative cross-linking/mass spectrometry analysis revealed unknown structure of complement iC3
We applied quantitative cross-linking/mass spectrometry (QCLMS) to interrogate the structure of iC3 (or C3(H2O)), the activated hydrolytic product of the abundant human complement protein C3. The slow but spontaneous and ubiquitous formation of iC3 from C3 initiates antibody-independent activation o...
ORGANISM(S): Homo sapiens (Human) 
2016-06-17 | PXD003486 | Pride
Quantitative cross-linking/mass spectrometry  domain architecture  activation of complement system  alternative pathway 
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