My talk will review recent work in my lab concerning molecular dynamics simulations of protein conformational landscapes for allostery and ligand binding; as well as the corresponding fitness landscapes. I will describe a new alchemical path for determining free energy differences between protein metastable states and relate these studies in conformational space to Potts Hamiltonian statistical models in sequence space to infer structural propensities of proteins. I will also describe our use of reweighting techniques to deal with hysteresis effects when constructing thermodynamic cycles involving protein allostery and binding.  Examples will be chosen from Kinase family proteins and HIV proteins.<br/>

Exploring free energy and fitness landscapes of proteins for allostery and binding

2019 Spring National Meeting

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