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From version 7.1
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16 16  
17 17  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.
18 18  
19 -[[Tong et al. (2016)>>url:https://doi.org/10.1002/prot.25167]]
19 +.. |doi_tong| raw:: html 
20 20  
21 +
22 + <a href="https:~/~/doi.org/10.1002/prot.25167" target="_blank">Tong et al (2016)</a>
23 +
21 21  == Procedure ==
22 22  
23 23  ~* 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.
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45 45  
46 46  == Related Jupyter Notebook ==
47 47  
48 -Please note: For technical reasons the notebooks currently are not running live in the collaboratory.
49 -
50 50  {{jupyterlink}}
51 51  https://lab.ebrains.eu/user-redirect/lab/tree/shared/Molecular%20Tools:%20protein%20association%20rates%20and%20binding%20sites/JN/Compare_a_region_of_the_electrostatic_potentials_of_a_set_of_protein_isoforms.ipynb
52 52  {{/jupyterlink}}