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...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2016-12-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340916306564 |
| Summary: | 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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| ISSN: | 2352-3409 |