Signal transduction using real proteins

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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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