Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.

ABSTRACT: Nickel-chelating lipids offer a convenient platform for reversible immobilization of histidine-tagged proteins to liposome surfaces. This interaction recently found utility as a model system for studying membrane remodeling triggered by protein crowding. Despite its wide array of utility, the molecular details of transient protein association to the lipid surfaces decorated with such chelator lipids remains poorly understood. In this study, we explore the kinetics of protein-liposome association across a wide concentration range using stopped-flow fluorescence. The fluorescence of histidine-tagged protein containing an intrinsic fluorophore (superfolder green fluorescent protein, SfGFP) was quenched upon binding to Ni-NTA-modified liposomes containing the quencher Dabsyl-PE lipids. Stopped

SUBMITTER: Raghunath G 

PROVIDER: S-EPMC6759406 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature