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

. 2018 Mar 28;8:5344. doi: 10.1038/s41598-018-23625-7

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

© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Concentration-dependent dimer-monomer exchanges in recombinant split-fluorescent proteins. (a) Schematic of dimer-monomer equilibrium in recombinantly produced sFPs. K_eq represents the equilibrium constant for dimer formation. (b) Size exclusion high-pressure liquid chromatography of non-complemented sGFP2 labeled with fluorescent ReAsH on an N-terminal tetracysteine tag. sGFP2 is mostly dimeric at 20 µM (apparent molecular weight of 61 KDa) but mostly monomeric at a lower concentration of 0.5 µM (apparent molecular weight of 31 KDa). The retention times of a set of calibrated molecular weight standards (68, 43, 29 and 14 KDa) are provided as reference. (c) Steady-state fluorescence anisotropy of ReAsH-labeled sGFP2 at different concentrations. The apparent equilibrium constant of dimer formation (K_eq) is determined by fitting the anisotropy curve with the inset equation (green), which describes the ensemble anisotropy contributed by both dimer anisotropy (rd) and monomer anisotropy (rm) at each total sGFP2 concentration. Anisotropy values are presented as mean ± std from measurements in triplicate.