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ProteomicsPASEF technology on timsTOF Pro improves quality of FPOP analysis
Fast photochemical oxidation of proteins (FPOP) is a modern technique for studying protein folding, conformations, interactions, etc. In this work, timsTOF Pro mass spectrometer coupled with trapped ion mobility spectrometry was used for identification of oxidative modifications in a model protein. ...
ORGANISM(S): Homo sapiens (Human) 
2021-06-10 | PXD020509 | Pride
Tims Pasef Timstof Protein footprinting Hydroxyl radical Fpop 
ProteomicsData-Independent Acquisition Represents a Promising Alternative for Fast Photochemical Oxidation of Proteins (FPOP) Samples Analysis
We propose a novel approach for FPOP data analysis, utilizing DIA data. The HbHp protein complex was analyzed by FPOP and measured on timsToF SCP in DIA, DDA and MS modes. The IDs of modified peptides were quantified for each acquisition mode and the extent of modification was calculated on the leve...
ORGANISM(S): Homo sapiens (Human) 
2024-07-08 | PXD050132 | Pride
Fast photochemical oxidation of proteins (fpop) Protein structure Protein footprinting Spectral library Hemoglobin-haptoglobin Data-independent acquisition (dia) 
ProteomicsFPOP of Daptomycin in Nanodiscs
FPOP data examining solvent exposure of daptomycin at different concentrations in the presence of nanodiscs with different lipids
ORGANISM(S): Bacteria (ncbitaxon:2) 
2022-11-01 | MSV000090629 | MassIVE
UnknownEfficient Analysis of Proteome-wide FPOP Data by FragPipe.
Not available
S-EPMC10274679 | biostudies-literature
ProteomicsHydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex
Methods of structural mass spectrometry have become more popular to study protein structure and dynamics. Among them, fast photochemical oxidation of proteins (FPOP) has several advantages such as irreversibility of modifications and more facile determination of the site of modification with single ...
ORGANISM(S): Homo sapiens (Human) 
2021-12-30 | PXD021621 | Pride
Footprinting Hemoglobin Haptoglobin Fpop Timstof pro 
ProteomicsMass Spectrometry Footprinting Reveals How Kinetic Stabilizers Counteract Transthyretin Dynamics Altered by Pathogenic Mutations_FPOP
Transthyretin (TTR) aggregation causes transthyretin amyloidosis, a severe condition often linked to mutations that destabilize the TTR tetramer, leading to amyloid fibril formation. Small molecules that stabilize the tetramer can prevent this process. While over 300 X-ray structures of TTR exist, t...
ORGANISM(S): Homo sapiens (Human) 
2025-12-13 | PXD071928 | Pride
Transthyretin Fast photochemical oxidation of proteins (fpop) Protein dynamics 37 hydrogen/deuterium exchange mass spectrometry (hdx-ms) 
ProteomicsStructural aspects of FOXO4 binding to DAF16 investigated with FPOP using both bottom-up and top-down MS.
A combination of covalent labelling techniques and mass spectrometry (MS) is currently a progressive approach for the de-riving insights relating to the mapping of protein surfaces or protein-ligand interactions. In this study, we mapped an interac-tion interface between DNA binding domain (DBD) of ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-14 | PXD027624 | Pride
Bottom-up proteomics Dna Transcription factors Protein Foxo4 Fast photochemical oxidation of proteins Top-dow proteomics 
ProteomicsMapping the binding site of VAR2CSA to chondroitin sulfate A
The FPOP was performed in order to map the binding site of chondroitin sulfate A to VAr2CSA from Plasmodium.
ORGANISM(S): Plasmodium falciparum FcB1/Columbia 
2021-04-09 | PXD024154 | Pride
Chondoitin sulfate a Hrpf Var2csa Fpop 
UnknownVariation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity.
Not available
S-EPMC6087495 | biostudies-literature
UnknownAn improved fast photochemical oxidation of proteins (FPOP) platform for protein therapeutics.
Not available
S-EPMC5993200 | biostudies-literature
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