Detailed understanding of how protein dynamics orchestrates function in cellular processes at atomic resolution remains ambiguous. Protein sequences and static three-dimensional structures alone are not always adequate to provide a complete understanding of protein function. We use atomistic molecular dynamics simulations to complement experiments to understand how conformational dynamics are coupled to protein allosteric mechanisms. In this talk, we will discuss a general strategy guided by molecular dynamics simulations to sense rapid endoplasmic reticulum calcium dynamics by tuning rapid protein dynamics to modulate the conformational ensemble and alter the residue-residue network. Additionally, we will discuss computational analysis of mapping key dynamical features as residue-residue contacts to detect distal allosteric effects. The results provide insights into the general interplay between protein dynamics and function from an atomistic perspective that have implications for structure-based drug design and protein engineering.

Tuning protein dynamics to sense calcium dynamics

ACS Spring 2022

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