Changes for page 2.3 Compare a specific region of the electrostatic potentials surrounding a set of protein isoforms with multipipsa

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  In this use case, we use as our input structure a structure of the catalytic domain of the enzyme adenylyl cyclase 5 (AC5), modelled during the work described in |doi_tong|.  The structures of the AC isoforms were created via homology modelling using the same template. The region where there are significant structural differences between the isoforms is in a flexible loop region that was not defined in the template structure. There are also variations in sequence length across AC isoforms in this region.
--.. |doi_tong| raw:: html
++[[Tong et al. (2016)>>url:https://doi.org/10.1002/prot.25167]]
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--    <a href="https:~/~/doi.org/10.1002/prot.25167" target="_blank">Tong et al (2016)</a>
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  == Procedure ==
  ~* Structure of AC5 is visualized. The catalytic domain of AC5 is a dimer consisting of two protein chains. In the full structure of AC5 these two chains are connected by a series of transmembrane helices that anchor the protein in the post-synaptic membrane.