Ontology highlight
ABSTRACT:
SUBMITTER: Jung HH
PROVIDER: S-EPMC2905102 | biostudies-literature | 2010 Jul
REPOSITORIES: biostudies-literature
Jung Hyun Ho HH Jung Hoi Jong HJ Milescu Mirela M Lee Chul Won CW Lee Seungkyu S Lee Ju Yeon JY Eu Young-Jae YJ Kim Ha Hyung HH Swartz Kenton J KJ Kim Jae Il JI
Biophysical journal 20100701 2
Amphipathic protein toxins from tarantula venom inhibit voltage-activated potassium (Kv) channels by binding to a critical helix-turn-helix motif termed the voltage sensor paddle. Although these toxins partition into membranes to bind the paddle motif, their structure and orientation within the membrane are unknown. We investigated the interaction of a tarantula toxin named SGTx with membranes using both fluorescence and NMR spectroscopy. Depth-dependent fluorescence-quenching experiments with b ...[more]