Andrew Plested<p>Are you interested in <a href="https://mstdn.science/tags/Calmodulin" class="mention hashtag" rel="tag">#<span>Calmodulin</span></a> (CaM) and its interaction with CaMKII? We had a look at this interaction with <a href="https://mstdn.science/tags/photocrosslinking" class="mention hashtag" rel="tag">#<span>photocrosslinking</span></a>. Covalent attachment of CaM did not break apart the CaMKII holoenzyme but did promote ongoing <a href="https://mstdn.science/tags/kinase" class="mention hashtag" rel="tag">#<span>kinase</span></a> activity. The CaM binding segment is also more mobile than expected from previous reports. </p><p>This is the accepted pdf, a long time in the making as you might detect. <br /><a href="https://onlinelibrary.wiley.com/doi/abs/10.1002/pro.4798" target="_blank" rel="nofollow noopener" translate="no"><span class="invisible">https://</span><span class="ellipsis">onlinelibrary.wiley.com/doi/ab</span><span class="invisible">s/10.1002/pro.4798</span></a></p><p><a href="https://mstdn.science/tags/Biophysics" class="mention hashtag" rel="tag">#<span>Biophysics</span></a> <a href="https://mstdn.science/tags/Biochemistry" class="mention hashtag" rel="tag">#<span>Biochemistry</span></a> <a href="https://mstdn.science/tags/Neuroscience" class="mention hashtag" rel="tag">#<span>Neuroscience</span></a> <a href="https://mstdn.science/tags/MassPhotometry" class="mention hashtag" rel="tag">#<span>MassPhotometry</span></a></p>