Data provided by National Institute of Standards and Technology
This database gives hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, Fc(gamma)RIa (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils. The working datasets comprise 17,750 deuterium uptake measurements in peptides from the receptor and the light and heavy chains of aIL8hFc obtained during 7 experiments, each comprising three runs of six exchange times. The data illuminate on the hydrogen exchange dynamics in isolated receptor, isolated IgG1 glycoforms, and receptor-IgG1 complexes.
About this Dataset
Updated: 2024-02-22
Metadata Last Updated:
2021-02-17 00:00:00
Date Created:
N/A
Data Provided by:
Dataset Owner:
N/A
| Title | Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the Fc(gamma)RIa (CD64) Receptor |
|---|---|
| Description | This database gives hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, Fc(gamma)RIa (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils. The working datasets comprise 17,750 deuterium uptake measurements in peptides from the receptor and the light and heavy chains of aIL8hFc obtained during 7 experiments, each comprising three runs of six exchange times. The data illuminate on the hydrogen exchange dynamics in isolated receptor, isolated IgG1 glycoforms, and receptor-IgG1 complexes. |
| Modified | 2021-02-17 00:00:00 |
| Publisher Name | National Institute of Standards and Technology |
| Contact | mailto:[email protected] |
| Keywords | antibody-receptor interaction , chromatography , HDX-MS , hydrogen-deuterium exchange , glycosylation , mass spectrometry , monoclonal antibody , precision , peptide , protein , proteolysis , proteomics , receptor. |
{
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"contactPoint": {
"hasEmail": "mailto:[email protected]",
"fn": "Jeffrey W. Hudgens"
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"programCode": [
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"landingPage": "",
"title": "Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the Fc(gamma)RIa (CD64) Receptor",
"description": "This database gives hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, Fc(gamma)RIa (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils. The working datasets comprise 17,750 deuterium uptake measurements in peptides from the receptor and the light and heavy chains of aIL8hFc obtained during 7 experiments, each comprising three runs of six exchange times. The data illuminate on the hydrogen exchange dynamics in isolated receptor, isolated IgG1 glycoforms, and receptor-IgG1 complexes.",
"language": [
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],
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"title": "SHA256 File for HDX-MS data for peptides from the light chain of holo-aIL8hFc SAF glycoform in complexation with Fc(gamma)R1a."
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"title": "SHA256 File for HDX-MS data of peptides from isolated (apo-)Fc(gamma)R1a."
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{
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{
"downloadURL": "https:\/\/data.nist.gov\/od\/ds\/mds2-2365\/Sequences%20of%20aILhFc%20and%20soluble%20FcgR1a%20%28CD64a%29.pdf.sha256",
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"title": "SHA256 File for Sequences of aILhFc and soluble FcgR1a (CD64a)"
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{
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{
"accessURL": "https:\/\/doi.org\/10.18434\/mds2-2365",
"title": "DOI Access for Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the Fc(gamma)RIa (CD64) Receptor"
}
],
"bureauCode": [
"006:55"
],
"modified": "2021-02-17 00:00:00",
"publisher": {
"@type": "org:Organization",
"name": "National Institute of Standards and Technology"
},
"theme": [
"Bioscience:Proteomics",
"Chemistry:Analytical chemistry",
"Bioscience:Biomaterials",
"Chemistry:Molecular characterization",
"Health:Pharmaceuticals",
"Manufacturing:Biomanufacturing",
"Materials:Materials characterization"
],
"keyword": [
"antibody-receptor interaction",
"chromatography",
"HDX-MS",
"hydrogen-deuterium exchange",
"glycosylation",
"mass spectrometry",
"monoclonal antibody",
"precision",
"peptide",
"protein",
"proteolysis",
"proteomics",
"receptor."
]
}
