Ontology highlight
ABSTRACT:
SUBMITTER: Zachariae U
PROVIDER: S-EPMC2373638 | biostudies-literature | 2002 Jun
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20020601 6
The functional properties of the anion-selective porin Omp32 from the bacterium Delftia acidovorans, formerly Comamonas acidovorans, are determined by the particularly narrow channel constriction and the electrostatic field inside and outside the pore. A cluster of arginines (Arg 38, Arg 75, and Arg 133) determines the electrostatic field close to the constriction zone. Stacked amino acids carrying charges are prone to drastic pK(a) shifts. However, optimized calculations of the titration behavi ...[more]