Hi,

I have a protein modelled in alphafold2. The protein has a couple of substituted amino acids, to try and improve its solubility and increase its hydrophilicity

• How would you go about measuring if it is in fact more soluble and more hydrophilic after the substitutions, in comparison to the original non-substituted protein?
• Are there any tools that can predict if the substitutions might negatively alter the structure of the protein? Such as increased aggregation or steric hindrance.

Thank you!

Best, A