Despite their lack of permanent tertiary structure, intrinsically disordered regions in proteins carry out a range of important biological functions. By using molecular dynamics simulations and hydration free energy calculations, Awile et al. (doi:10.1371/journal.pcbi.1000854) demonstrate that the intrinsically disordered regions in the enzyme nudix hydrolase from the desiccation- and radiation-resistant bacterium Deinococcus radiodurans may play an important role in keeping this key enzyme hydrated under extreme desiccation. This idealized artistic rendering shows a possible scenario whereby nudix hydrolase remains in a droplet of residual water due to its hydrophilic disordered regions, while other less hydrophilic proteins are forced out of solution.
Image Credit: Omar Awile
Perspective
The Roots of Bioinformatics in Protein Evolution
PLOS Computational Biology: published July 29, 2010 | https://doi.org/10.1371/journal.pcbi.1000875
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