Monday, May 20, 2019
The pH responding proteins
The changes in the environment acidity may lead to important protein conformational changes, even unfolding. Accounting for this effect in silico is a real challenge. A recent paper from the group of D. Baker shows how by modelling the distribution of histidine residues in the network of hydrogen bonds that stabilises the fold of a protein is possible to control the response of a protein to pH changes. The paper is out in the Science magazine here. The possibility to account in simulations for pH has inspired also several computational approaches along the years. Very recently titration method combined to coarse-grained MD simulations was demonstrated to be a cheap but effective strategy in both the simulation of RNA [see Pasquali et al, Interface Focus, 2019, here] and proteins [see Barroso et al, JCTC, 2019, here].
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