Peripheral Protein Unfolding Drives Membrane Bending.
Ontology highlight
ABSTRACT: Dynamic modulation of lipid membrane curvature can be achieved by a number of peripheral protein binding mechanisms such as hydrophobic insertion of amphipathic helices and membrane scaffolding. Recently, an alternative mechanism was proposed in which crowding of peripherally bound proteins induces membrane curvature through steric pressure generated by lateral collisions. This effect was enhanced using intrinsically disordered proteins that possess high hydrodynamic radii, prompting us to explore whether membrane bending can be triggered by the folding-unfolding transition of surface-bound proteins. We utilized histidine-tagged human serum albumin bound to Ni-NTA-DGS containing liposomes as our model system to test this hypothesis. We found that reduction of the disulfide bonds in the pro
SUBMITTER: Siaw HMH
PROVIDER: S-EPMC6069603 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
ACCESS DATA