Probing the Location and Dynamics of the sensor of a Voltage-Gated Channel
Abstract
The research is aimed at eventually determining the molecular mechanism by which the channel-forming membrane protein, VDAC, is voltage dependent. VDAC is located in the outer membrane of mitochondria from all species and its properties are highly conserved. The mitochondria of yeast and N. crassa were the major sources of VDAC for the work reported here. The research effort has moved toward the long-term goal stated above by examining agents that probe VDAC's gating process. Metal trihydroxides strongly inhibit the gating process by effectively neutralizing the voltage sensor that allows VDAC to respond to the membrane potential. Other metal species in solution and metals of lower that valance 3 are inactive. Active metals include aluminum, gallium, indium, scandium, ajd chromium. Membrane channel, Voltage dependence, Aluminum, Polyanion, Protein modification, Mitochondrion, Outer membrane, Selectivity, Mutations.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 21, 1988
- Accession Number
- ADA199621
Entities
People
- Marco Colombini
Organizations
- University of Maryland