I am working on two protein, eg. A and B. Both are having 10% sequence identity but the three dimentional structural similarity is about 90%.
It is expected that both these proteins may follow similar folding patterns irrespective of their amino acid sequences. Identifying those similar patterns that result from non-covalent interactions like hydrophobic interactions, electrostatic/ionic interactions, hydrogen bonding and disulphide bonds will be a critical study to understand the folding pathway of the proteins. Namely, the objective of this study is to understand what makes two different protein polypeptide chain fold to a similar structure.