Ontology highlight
ABSTRACT:
SUBMITTER: Kubala M
PROVIDER: S-EPMC2741587 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Kubala Martin M Grycova Lenka L Lansky Zdenek Z Sklenovsky Petr P Janovska Marika M Otyepka Michal M Teisinger Jan J
Biophysical journal 20090901 6
A set of single-tryptophan mutants of the Na(+)/K(+)-ATPase isolated, large cytoplasmic loop connecting transmembrane helices M4 and M5 (C45) was prepared to monitor effects of the natural cytoplasmic ligands (i.e., Mg(2+) and/or ATP) binding. We introduced a novel method for the monitoring of the changes in the electrostatic surface potential (ESP) induced by ligand binding, using the quenching of the intrinsic tryptophan fluorescence by acrylamide or iodide. This approach opens a new way to un ...[more]