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SUMMARY:Design of Hinge Proteins for the Population of Two Conformational S
 tates
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20251120T160000
UID:2026-06-13-05-44-17@natsci.colostate.edu
DTSTAMP:20260613T054417
Description:About the seminar:\n\nProteins that adopt distinct conformation
 s in response to environmental cues are common in nature\; for example\, h
 emoglobin changes shape when it binds oxygen\, and ion channels open or cl
 ose in response to changes in voltage. Creating proteins that switch betwe
 en two stable conformations is challenging because it involves optimizing 
 a single protein to adopt two stable states\, or two prominent minima on t
 he 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 co
 nformations. This enables designers to manipulate the energy landscape of 
 molecular systems to control their dynamics. The hinge protein design pres
 ented here offers a versatile approach applicable to various systems\, suc
 h as molecular sensors for detecting metabolites or components for large m
 olecular machines\, moving beyond the traditional static\, one-state struc
 tures. 4:00 pm
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