<p>Continuing from the title, in my context, important means that changing the set of AAs (either or one more many) changes the domain and/or fold and/or function and/or family etc.</p>
<p>I  noticed that there are two types of methods Protbert (protein language models, sequence-based methods) and/or Alphafold (structure (tertiary) based methods); one needs both methods to &quot;reallY&quot; identify the essential set of AAs in a given protein?
Thanks</p>

CC BY-SA 4.0
2022-06-11T20:24:15.097Z
Please edit the question to limit it to a specific problem with enough detail to identify an adequate answer.
Community
CC BY-SA 4.0
2022-06-12T12:50:24.903Z
Sorry. This question is ill posed as it completely depends on context —namely is simply a question of **what are the main roles AA residues can take**. Core residues when mutated may cause and increase in Gibbs free energy of folding (i.e. less energy is released when folded from a magically linear protein form), these are key to Structure as seen in **PDB** and predicted by Alphafold. Catalytic residues are key to activity. Channel gate residues are key to permeability. etc etc etc etc
Matteo Ferla
CC BY-SA 4.0
2022-06-12T17:15:46.820Z
Do you have many examples of your protein from different species? Can you look at alignments of the various homologs?
terdon
<phylogenetics><protein-structure>
How to identify most important Amino Acid residues in a given protein?
# How to identify most important Amino Acid residues in a given protein?

(Asked by: username_0 on 2022-06-11)

Continuing from the title, in my context, important means that changing the set of AAs (either or one more many) changes the domain and/or fold and/or function and/or family etc.

I noticed that there are two types of methods Protbert (protein language models, sequence-based methods) and/or Alphafold (structure (tertiary) based methods); one needs both methods to "reallY" identify the essential set of AAs in a given protein?
Thanks

**Tags:** phylogenetics, protein-structure
> **Comments:**
> **username_1**: Please edit the question to limit it to a specific problem with enough detail to identify an adequate answer.  
> **username_2**: Sorry. This question is ill posed as it completely depends on context —namely is simply a question of **what are the main roles AA residues can take**. Core residues when mutated may cause and increase in Gibbs free energy of folding (i.e. less energy is released when folded from a magically linear protein form), these are key to Structure as seen in **PDB** and predicted by Alphafold. Catalytic residues are key to activity. Channel gate residues are key to permeability. etc etc etc etc  
> **username_3**: Do you have many examples of your protein from different species? Can you look at alignments of the various homologs?  

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## 0 answers

