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Intrinsically disordered regions may increase the overall hydrophilicity of key proteins in desiccation-resistant organisms.
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
Citation: (2010) PLoS Computational Biology Issue Image | Vol. 6(7) July 2010. PLoS Comput Biol 6(7): ev06.i07. https://doi.org/10.1371/image.pcbi.v06.i07
Published: July 29, 2010
Copyright: © 2010 Awile et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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