Studying co-chaperone hHep1 interactions with membranes using TR-SAXS and stopped-flow rapid mixing

ssues related to protein misfolding and aggregation are central in diverse pathologies, from human diseases to cell stress adaptation failure by bacteria, and are a topic of interest for both fundamental and applied research. Proteins central in protein misfolding issue corrections are the molecular chaperones, essential for cell survival, which may also indirectly effect other processes. One such protein is the Hsp70-escort protein (hHep1), which has chaperone functions but is also essential for mitochondrial protein import. Here, we propose Time-Resolved Small Angle X-Ray Scattering (TR-SAXS) to address the role hHep1 has in this import process by using a stopped-flow rapid mixing setup, and to vary parameters such as membrane composition and temperature to simulate the mitochondrial membrane in different fluidity levels.