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Hydrogen/deuterium exchange mass spectrometric methods for protein structural analysis are conventionally performed in solution. We present Tissue Deuterium Exchange Mass Spectrometry (TDXMS), a method to directly monitor deuterium uptake on tissue, as a means to better approximate the deuterium exc...
ORGANISM(S): Rattus norvegicus (Rat) 
2016-08-15 | PXD004630 | Pride
We have performed in solution hydrogen exchange (HDX) on peptide standards and bovine hemoglobin with subsequent quenching, pepsin digestion, and cold capillary electrophoretic separation coupled with mass spectrometry (MS) detection for the benchmarking of a lab built HDX-MS platform. Though neutra...
ORGANISM(S): Bos taurus (Bovine) 
2022-12-22 | PXD034245 | Pride
Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is a powerful protein footprinting technique to study protein dynamics and binding; however, HDX-MS data analysis is often challenging and time consuming. Moreover, the HDX community is expanding to investigate multi-protein and highly complex p...
ORGANISM(S): Escherichia coli 
2023-01-30 | PXD036813 | Pride
Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS) has been widely adopted as part of the drug development pipeline, frequently used in both the development of biopharmaceuticals and small molecule compound development to assess target engagement spatially. Frequently, HDX-MS analyses are conduc...
ORGANISM(S): Plasmodium falciparum 58.1 
2026-04-01 | PXD070051 | Pride
Antibody light chains can aggregate as amyloid fibrils to cause systemic AL amyloidosis. Amyloid deposition requires unfolding of the light chain from its native state, but the mechanistic details of how this occurs are not fully understood. Inhibiting amyloid formation by stabilizing the precursor ...
ORGANISM(S): Homo sapiens (Human) 
2026-07-27 | PXD068745 | Pride
To monitor the structural integrity of therapeutic proteins, hydrogen-deuterium exchange mass spectrometry (HDX-MS) is increasingly utilized in the pharmaceutical industry. The successful outcome of HDX-MS analyses depends on the sample preparation conditions, which involve the rapid digestion of pr...
ORGANISM(S): Escherichia coli 
2017-07-12 | PXD006766 | Pride
CysE and CysK, the last two enzymes of the cysteine biosynthetic pathway, engage in a bienzyme complex, cysteine synthase (CS), with yet incompletely characterized three-dimensional structure and regulatory function. Being absent in mammals, the two enzymes and their complex are attractive targets f...
ORGANISM(S): Escherichia coli 
2021-06-07 | PXD025300 | Pride
Mtr4 is a eukaryotic RNA helicase required for RNA decay by the nuclear exosome. Previous studies have shown how RNA enroute to the exosome threads through the highly conserved helicase core of Mtr4. Mtr4 also contains an arch domain, although details of potential interactions between the arch and R...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-03-07 | PXD031962 | Pride
General control nonderepressible 2 (GCN2) phosphorylates eIF2α, regulating translation in response to nutritional stress. Here, we show that mammalian ribosomes are potent GCN2 activators. Hydrogen/deuterium exchange–mass spectrometry (HDX-MS) showed GCN2 interacting with domain II of the uL10 P-sta...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2019-05-24 | PXD013051 | Pride
The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the ra...
ORGANISM(S): Escherichia coli 
2020-01-15 | PXD016509 | Pride
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