Filtering by
- All Subjects: ATP Synthase
- Creators: Fromme, Petra
- Creators: Redding, Kevin
θATP-bd exists. The ATP-binding dwell can occur even at saturating ATP concentrations. We report that ω follows a distinct pattern in the vicinity of the ATP-binding dwell, and that the ω(θ) curve contains the same oscillations within it regardless of θATP-bd. We observed that an acceleration/deceleration dependence before and after the ATP-binding dwell, respectively, remained for increasing time intervals as the dwell occurred later in Phase-1, to a maximum of ≈ 40°. The results were interpreted in terms of a model in which the ATP-binding dwell results from internal drag at a variable position on the γε rotor.
Diisobutylene maleic acid, or DIBMA, offers a novel approach to integral membrane protein extraction without requiring the use of detergent. This copolymer extracts the protein along with the surrounding lipids, creating native nanodiscs. This method of solubilization is the preferred method, as traditional detergent solubilization can possibly alter the structural and functional integrity of the membrane protein. DIBMA solubilization, on the other hand, is able to create a more stable environment for the integral membrane protein, while allowing purification through commonly used chromatography methods similar to established detergent solubilization protocols. In this project, we study the ability of DIBMA to isolate the integral membrane protein, chloroplast ATP synthase, without the use of detergents.