Uploaded April 2026 | Updated September 2026, 2 weeks ago
Proteins have long been modeled as mechanical networks of nodes connected by springs. We have studied the inverse problem, of starting with mechanical networks and then tuning their properties to introduce protein function. We focus on allostery, where binding of a small molecule to the protein triggers a conformational change that enables binding or unbinding of another small molecule. Here I will describe what our approach brings to protein allostery, including a relation between structure and function and insight into the phenomenon of global epistasis, where the non-additivity of mutations can have a global contribution, arising from the cost landscape in which the mutation occurs.
For more information please visit: simonsfoundation.org/event/national-institute-for-theory-and-mathematics-in-biology-annual-meeting-2026
Proteins have long been modeled as mechanical networks of nodes connected by springs. We have studied the inverse problem, of starting with mechanical networks and then tuning their properties to introduce protein function. We focus on allostery, where binding of a small molecule to the protein triggers a conformational change that enables binding or unbinding of another small molecule. Here I will describe what our approach brings to protein allostery, including a relation between structure and function and insight into the phenomenon of global epistasis, where the non-additivity of mutations can have a global contribution, arising from the cost landscape in which the mutation occurs.
For more information please visit: simonsfoundation.org/event/national-institute-for-theory-and-mathematics-in-biology-annual-meeting-2026
