ArticleLangmuir : the ACS journal of surfaces and colloids2019
Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.
Article in Langmuir : the ACS journal of surfaces and colloids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
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- SPOT-RASTR-A cryo-EM specimen preparation technique that overcomes problems with preferred orientation and the air/water interface.PNAS nexus · 2024Article
- Probing macromolecular crowding at the lipid membrane interface with genetically-encoded sensors.Protein science : a publication of the Protein Society · 2023Article
- Tuning Targeted Liposome Avidity to Cells via Lipid Phase Separation.Biomacromolecules · 2023Article
- Actomyosin-Driven Division of a Synthetic Cell.ACS synthetic biology · 2022Review
- Observed steric crowding at modest coverage requires a particular membrane-binding scheme or a complementary mechanism.Biophysical journal · 2022Article
- Influenza A virus hemagglutinin prevents extensive membrane damage upon dehydration.BBA advances · 2022Article
- Dynamic spatial and structural organization in artificial cells regulates signal processing by protein scaffolding.Chemical science · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
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-flow fluorescence reveals a complex, multiexponential binding behavior with a fast (
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Registered trials
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