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
Descripción
Sumario: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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