Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation

This article presented the data related to the research article entitled “Calibration-free concentration analysis for an analyte prone to self-association” (H. Imamura, S. Honda, 2017) [1]. The data included surface plasmon resonance (SPR) responses of the variants of protein G with different masses...

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Detalles Bibliográficos
Autores principales: Imamura, Hiroshi, Honda, Shinya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5114526/
https://www.ncbi.nlm.nih.gov/pubmed/27882339
http://dx.doi.org/10.1016/j.dib.2016.10.029
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author Imamura, Hiroshi
Honda, Shinya
author_facet Imamura, Hiroshi
Honda, Shinya
author_sort Imamura, Hiroshi
collection PubMed
description This article presented the data related to the research article entitled “Calibration-free concentration analysis for an analyte prone to self-association” (H. Imamura, S. Honda, 2017) [1]. The data included surface plasmon resonance (SPR) responses of the variants of protein G with different masses under mass transport limitation. The friction factors of the proteins analyzed by an ultracentrifugation were recorded. Calculation of the SPR response of the proteins was also described.
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spelling pubmed-51145262016-11-23 Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation Imamura, Hiroshi Honda, Shinya Data Brief Data Article This article presented the data related to the research article entitled “Calibration-free concentration analysis for an analyte prone to self-association” (H. Imamura, S. Honda, 2017) [1]. The data included surface plasmon resonance (SPR) responses of the variants of protein G with different masses under mass transport limitation. The friction factors of the proteins analyzed by an ultracentrifugation were recorded. Calculation of the SPR response of the proteins was also described. Elsevier 2016-11-05 /pmc/articles/PMC5114526/ /pubmed/27882339 http://dx.doi.org/10.1016/j.dib.2016.10.029 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Imamura, Hiroshi
Honda, Shinya
Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title_full Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title_fullStr Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title_full_unstemmed Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title_short Surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein G under mass transport limitation
title_sort surface plasmon resonance biosensing of the monomer and the linked dimer of the variants of protein g under mass transport limitation
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5114526/
https://www.ncbi.nlm.nih.gov/pubmed/27882339
http://dx.doi.org/10.1016/j.dib.2016.10.029
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