ArticleBiophysical journal2021
Functional integrity of membrane protein rhodopsin solubilized by styrene-maleic acid copolymer.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Lipid packing is disrupted in copolymeric nanodiscs compared with intact membranes.Biophysical journal · 2023Article
- Conformational Variability in Ground-State CFTR Lipoprotein Particle Cryo-EM Ensembles.International journal of molecular sciences · 2022Article
- Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review.Nanomaterials (Basel, Switzerland) · 2022Review
- Styrene-maleic acid copolymer effects on the function of the GPCR rhodopsin in lipid nanoparticles.Biophysical journal · 2021Article
- Squaring off with G protein-coupled receptors function in polymer nanoscale lipid bilayers.Biophysical journal · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane proteins often require solubilization to study their structure or define the mechanisms underlying their function. In this study, the functional properties of the membrane protein rhodopsin in its native lipid environment were investigated after being solubilized with styrene-maleic acid (SMA) copolymer. The static absorption spectra of rhodopsin before and after the addition of SMA were recorded at room temperature to quantify the amount of membrane protein solubilized. The samples were then photobleached to analyze the functionality of rhodopsin upon solubilization. Samples with low or high SMA/rhodopsin ratios were compared to find a threshold in which the maximal amount of active rhodopsin was solubilized from membrane suspensions. Interestingly, whereas the highest SMA/rhodopsin ratios yielded the most solubilized rhodopsin, the rhodopsin produced under these conditions could not reach the active (Meta II) state upon photoactivation. The results confirm that SMA is a useful tool for membrane protein research, but SMA added in excess can interfere with the dynamics of protein activation.
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Registered trials
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