Open Conference Systems, StatPhys 27 Main Conference

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Protein Non-folding as a Regulatory Phenomenon
Carlos J. Camacho

##manager.scheduler.building##: Edificio San Jose
##manager.scheduler.room##: Auditorio 1
Date: 2019-07-08 04:00 PM – 04:15 PM
Last modified: 2019-06-10

Abstract


A large number of proteins are sufficiently unstable that their full 3D structure cannot be resolved. The origins of this intrinsic disorder are not well understood, but its ubiquitous presence undercuts the principle that a protein’s structure determines its function. In this presentation, I will show how thermodynamics principles demonstrate that, without assuming any a priori structure–function relationship, both catalytic and low-affinity binding (Kd ~ 10-7 M) proteins prefer ordered structures, whereas only high-affinity binding proteins (found mostly in eukaryotes) can tolerate disorder. Relevant to both transcription and signal transduction, the theory also explains how increasing disorder can tune the binding affinity to maximize the specificity of promiscuous interactions. Collectively, these studies provide insight into how natural selection acts on folding stability to optimize the function of proteins with multiple partners.