About the seminar:

Proteins that adopt distinct conformations in response to environmental cues are common in nature; for example, hemoglobin changes shape when it binds oxygen, and ion channels open or close in response to changes in voltage. Creating proteins that switch between two stable conformations is challenging because it involves optimizing a single protein to adopt two stable states, or two prominent minima on the energy landscape. This work demonstrates that, by employing stringent design criteria, advanced optimization algorithms, and machine learning models, scientists can now effectively design proteins with two stable conformations. This enables designers to manipulate the energy landscape of molecular systems to control their dynamics. The hinge protein design presented here offers a versatile approach applicable to various systems, such as molecular sensors for detecting metabolites or components for large molecular machines, moving beyond the traditional static, one-state structures.