Sort   by:  
 Page size 
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 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
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
Hydrogen-Deuterium Exchange Reveals Catalytically Linked Protein Flexibility
ORGANISM(S): Escherichia coli 
2025-12-29 | PXD071026 | Pride
Hydrogen/deuterium exchange (HDX) methods for studying protein dynamics would benefit from millisecond-scale incubations to probe intrinsically disordered proteins, highly dynamic regions and conformation changes. Here we investigate droplet microfluidics for rapid mixing to trigger D2O labelling, u...
ORGANISM(S): Bos taurus (Bovine) 
2025-06-23 | PXD063880 | Pride
Characterizing and distinguishing protein-ligand interactions is crucial for understanding cellular metabolism and guiding drug discovery and development. We employ hydrogen/deuterium exchange mass spectrometry (HDX-MS) and a new Fenton chemistry-based approach to protein oxidative mass spectrometry...
ORGANISM(S): Homo sapiens (Human) 
2026-03-27 | PXD050663 | Pride
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in E. coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES. We analyzed the spontaneous and chaperonin-assisted folding of the essen...
ORGANISM(S): Escherichia coli 
2020-03-05 | PXD016666 | 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
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
During the analysis steps of hydrogen deuterium exchange (HDX) mass spectrometry (MS) there is an unavoidable loss of deuterons, or back-exchange. Understanding back-exchange is necessary to correct for loss during analysis, to calculate the absolute amount of exchange, and to ensure that deuterium ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Equus caballus (Horse) 
2022-07-08 | PXD032924 | Pride
Sort   by:  
 Page size