Ontology highlight
ABSTRACT:
SUBMITTER: Tworowski D
PROVIDER: S-EPMC2323892 | biostudies-literature | 2003 Jun
REPOSITORIES: biostudies-literature
Tworowski Dmitry D Safro Mark M
Protein science : a publication of the Protein Society 20030601 6
In most cases aminoacyl-tRNA synthetases (aaRSs) are negatively charged, as are the tRNA substrates. It is apparent that there are driving forces that provide a long-range attraction between like charge aaRS and tRNA, and ensure formation of "close encounters." Based on numerical solutions to the nonlinear Poisson-Boltzmann equation, we evaluated the electrostatic potential generated by different aaRSs. The 3D-isopotential surfaces calculated for different aaRSs at 0.01 kT/e contour level reveal ...[more]