ArticleBiochemistry2011
In vitro folding of KvAP, a voltage-gated K+ channel.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- A Cost-EffectiveBioengineering (Basel, Switzerland) · 2024Article
- Structures of Gating Intermediates in a KJournal of molecular biology · 2021Article
- Expression, Purification and Refolding of a Human NaToxins · 2021Article
- Folding and misfolding of potassium channel monomers during assembly and tetramerization.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Shared Mechanism for the Folding of Voltage-Gated KBiochemistry · 2019Article
- Article
- High-yield production of "difficult-to-express" proteins in a continuous exchange cell-free system based on CHO cell lysates.Scientific reports · 2017Article
- Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.Biochemistry · 2016Article
- Shock Wave-Induced Damage of a Protein by Void Collapse.Biophysical journal · 2016Article
- Engineering the glutamate transporter homologue GltPh using protein semisynthesis.Biochemistry · 2015Article
- Semisynthetic K+ channels show that the constricted conformation of the selectivity filter is not the C-type inactivated state.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel.Scientific reports · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
In this contribution, we report in vitro folding of the archaebacterial voltage-gated K(+) channel, K(v)AP. We show that in vitro folding of the K(v)AP channel from the extensively unfolded state requires lipid vesicles and that the refolded channel is biochemically and functionally similar to the native channel. The in vitro folding process is slow at room temperature, and the folding yield depends on the composition of the lipid bilayer. The major factor influencing refolding is temperature, and almost quantitative refolding of the K(v)AP channel is observed at 80 °C. To differentiate between insertion into the bilayer and folding within the bilayer, we developed a cysteine protection assay. Using this assay, we demonstrate that insertion of the unfolded protein into the bilayer is relatively fast at room temperature and independent of lipid composition, suggesting that temperature and bilayer composition influence folding within the bilayer. Further, we demonstrate that in vitro folding provides an effective method for obtaining high yields of the native channel. Our studies suggest that the K(v)AP channel provides a good model system for investigating the folding of a multidomain integral membrane protein.
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