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. 2023 Feb 22;11:1105657. doi: 10.3389/fcell.2023.1105657

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Copyright © 2023 Radhakrishnan, Leung, Solanki and Lobo.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Surface plasmon resonance binding studies between mutant RBPR2 and its ligand RBP4. Binding studies using SPR between mouse RBPR2-S294A (A), RBPR2-Y295P (B), RBPR2-L296S (C) and immobilized mouse RBP4 protein is shown, together with the respective kinetic values (K _d) in the bottom respective panels. The interaction levels measured in Response Units (RU) and real time plot sensorgram display the dynamics of the analysis.