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

. 2021 Feb 25;296:100471. doi: 10.1016/j.jbc.2021.100471

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

© 2021 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Effects of S1 binding to pyrene-labeled F-actin (PFA) in the absence and presence of nucleotides.A, fluorescence spectra of 2 μM PFA (black) as a function of [S1] in the absence (green) and presence (red) of 1 mM Mg.ATP. B, inhibition of PFA fluorescence (at 407 nm) as a function of [S1] () and restoration by 1 mM MgATP (•). We also show the effects of forming the Mg.ADP.VO₄ () and Mg.PP_i () complexes in equimolar PFA-S1 (2 μM). The PFA fluorescence of S1:Actin (0.7:1 M ratio) is shown as a green data point ().

Inline graphic — Effects of S1 binding to pyrene-labeled F-actin (PFA) in the absence and presence of nucleotides.A, fluorescence spectra of 2 μM PFA (black) as a function of [S1] in the absence (green) and presence (red) of 1 mM Mg.ATP. B, inhibition of PFA fluorescence (at 407 nm) as a function of [S1] () and restoration by 1 mM MgATP (•). We also show the effects of forming the Mg.ADP.VO₄ () and Mg.PP_i () complexes in equimolar PFA-S1 (2 μM). The PFA fluorescence of S1:Actin (0.7:1 M ratio) is shown as a green data point ().