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Signal transduction using real proteins

From Santa Fe Institute Events Wiki

By Michael Wall, LANL.

Cells use networks of interacting proteins to maintain homeostasis, orchestrate developmental processes, and adapt to environmental changes. A primary mechanism of signal transduction in cellular networks is allostery, in which molecular interactions influence protein activity through changes in protein structure. In traditional models of allostery, proteins adopt a limited number of well-defined conformations. However, real proteins fluctuate in thermal equilibrium, dynamically exploring microstates with diverse activity.
In this talk I will examine the role of protein fluctuations in molecular interactions and allostery. Along the way I will describe recent insights into the induced fit vs. pre-existing equlibrium perspectives on binding and the evolution of protein functional sites. Finally, I will discuss some aspects of how protein fluctuations influence elementary steps in cellular signal transduction.

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