Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2013 Dec;54(12):3531–3538. doi: 10.1194/jlr.D041376

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2013 by the American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

Fig. 2. — Determination of K_d for PDK1-PH-EGFP membrane binding by SPR analysis. A: Equilibrium sensorgrams for PDK1-PH-EGFP interacting with POPC/POPS/PtdIns(3,4,5)P₃ (77:20:3) vesicles. The protein concentration was 25, 50, 100, 150, 200, and 300 nM from bottom to top. B: Binding isotherms of PDK1-PH-EGFP with POPC/POPS/PtdIns(3,4,5)P₃ (77:20:3) vesicles. The binding isotherm was fit by nonlinear least-squares analysis using the equation: R_eq = R_max/(1 + K_d/[P]_o) where [P]_o, R_eq, and R_max are the total protein concentration, the near-equilibrium resonance unit (RU) value for each P₀, and the maximal R_eq value, respectively. R_max (460 ± 20) RU and K_d (44 ± 15 nM) values were used to construct the theoretical curve (solid line). C: Kinetic sensorgrams for PDK1-PH-EGFP, NHERF1-PDZ2-EGFP, and EGFP (500 nM each) interacting with POPC/POPS/PtdIns(3,4,5)P₃ (77:20:3) vesicles coated onto the L1 chip.