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

ABSTRACT: 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.

SUBMITTER: Imamura H

PROVIDER: S-EPMC5114526 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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

Imamura Hiroshi H Imamura Hiroshi H Honda Shinya S

Data in brief 20161105

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. ...[more]

PMID: 27882339

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