Last modified by richtesn on 2023/06/15 15:51
From version 5.1
edited by richtesn
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To version 8.1
edited by richtesn
on 2023/06/15 15:51
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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 -.. |doi_tong| raw:: html 
19 +[[Tong et al. (2016)>>url:https://doi.org/10.1002/prot.25167]]
20 20  
21 -
22 - <a href="https:~/~/doi.org/10.1002/prot.25167" target="_blank">Tong et al (2016)</a>
23 -
24 24  == Procedure ==
25 25  
26 26  ~* 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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48 48  
49 49  == Related Jupyter Notebook ==
50 50  
48 +Please note: In the lab where the notebook is running, please select the kernel: EBRAINS-23.02
49 +
51 51  {{jupyterlink}}
52 52  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
53 53  {{/jupyterlink}}