37 hydrogen/deuterium exchange mass spectrometry (hdx-ms)

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Aspergillus niger Prolyl endoprotease (An-PEP) for Hydrogen-Deuterium Exchange Mass Spectrometry and Protein Structural Studies

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

Revealing the dynamic allosteric changes required for formation of the cysteine synthase complex by hydrogen-deuterium exchange mass spectrometry

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

Cysteine biosynthesis Allosteric regulation E. coli Synapt g2-si Bienzyme complex Hydrogen deuterium exchange (hdx-ms) Protein-protein interactions Cysteine synthase

HDX-MS of Human Histidine Rich Glycoprotein (HRG)

Histidine rich glycoprotein (HRG) is a multi-domain plasma glycoprotein, which is implicated in numerous biological processes including immune regulation, angiogenesis, coagulation and fibrinolysis. Despite a diverse role of biological functions, structural investigations into HRG have yielded only ...

ORGANISM(S): Homo sapiens (Human) Escherichia coli

2025-11-06 | PXD065786 | Pride

Hrg Hdx-ms

Significance of Histidine Hydrogen-Deuterium Exchange Mass Spectrometry in Protein Structural Biology.

Not available

S-EPMC10813008 | biostudies-literature

Investigation of the Solid-State Interactions in Lyophilized Human G-CSF Using Hydrogen-Deuterium Exchange Mass Spectrometry.

Not available

S-EPMC10988552 | biostudies-literature

Differential Scanning Fluorimetry and Hydrogen Deuterium Exchange Mass Spectrometry to Monitor the Conformational Dynamics of NBD1 in Cystic Fibrosis.

Not available

S-EPMC8311558 | biostudies-literature

ANGPTL3/8 is an atypical unfoldase that regulates intravascular lipolysis by catalyzing unfolding of lipoprotein lipase as measured by hydrogen/deuterium exchange mass spectrometry (HDX-MS)

Lipoprotein lipase (LPL) carries out the lipolytic processing of triglyceride-rich lipoproteins (TRL) along the luminal surface of capillaries. LPL activity is regulated by angiopoietin-like proteins (ANGPTL3, ANGPTL4, and ANGPTL8), which control the delivery of TRL-derived lipid nutrients to tissue...

ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human)

2025-03-26 | PXD060125 | Pride

Gpihbp1 Angptl3/8 Lipoprotein lipase Intravascular lipolysis Hdx-ms

HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.

Not available

S-EPMC2642988 | biostudies-literature

HDX-MS implicates dynamic CD20 antigen binding to two discontinuous CDR regions in the NCD1.2 monoclonal antibody

A comparative canine-human therapeutics model is being developed in B-cell lymphoma through the generation of a hybridoma cell that produces a murine monoclonal antibody specific for canine CD20. The hybridoma cell produces two light chains, light chain-3 and light chain-7. However, the contribution...

ORGANISM(S): Canis lupus x Canis lupus familiaris

2021-09-09 | PXD018550 | Pride

Human Comparative medicine Lymphoma Monoclonal antibody Hdx Adept Phage display Cd20

Molecular determinant for MED1 interaction with the VDR-RXR heterodimer

To provide structural insights into the mechanism of the specific association of the coactivator MED1 with the Vitamin D nuclear (VDR)-RXR heterodimer, we used combined structural methods including X-ray crystallography, small angle X-ray scattering (SAXS), NMR, hydrogen-deuterium exchange coupled t...

ORGANISM(S): Homo sapiens (Human)

2021-02-10 | PXD019530 | Pride

Nuclear receptor Vdr-rxr Xl-ms Hdx-ms

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