Ability to redesign existing scaffolds to create binding interfaces in comparison to de novo binder design

Hello!

Thank you for publishing your work! I'm currently experimenting with your software, and I have some ideas in mind, but I am not sure to what extent they are practical and possible with RFdiffusion. As I am new to the protein design field, feel free to correct any assumptions I may have made; I would greatly appreciate any guidance.

I have a target protein and a highly stable scaffold protein; however, the scaffold protein was not designed to bind to this specific target, so no actual binding motif is present. Is it possible (and effective) to use the RFdiffusion protocol, such as motif scaffolding, to redesign some parts of the existing scaffold that face the target hotspot to create a binding interface? Or would it be more effective to use partial diffusion/fold conditioned binder design to create new, but structurally similar scaffolds? If I understand correctly, the latter approach will cause loss of the binder sequence, which might lead to a possible loss of stability compared to the original scaffold.
I apologize if I am missing something about presented pipelines.

Thank you!

The issue names motif scaffolding, partial diffusion, and fold-conditioned binder design but no files, tests, or implementation entry points. Start by reviewing those existing workflows and their documentation; done would require a decided, supported approach for redesigning an existing scaffold rather than de novo binder design.