Structural basis for the pore-forming activity of a complement-like toxin A detailed mechanism by which a pore-forming toxin forms gigantic membrane pores using structural biology is reported.

Structural basis for the pore-forming activity of a complement-like toxin | Science Advances www.science.org/doi/full/10.... #poreformingtoxins

AlphaFold can be used to predict the oligomeric states of proteins www.biorxiv.org/cont...

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#proteomics #prot-preprint

A conceptual framework for understanding phase separation and addressing open questions and challenges Macromolecular phase separation is being recognized for its potential importance and relevance as a driver of spatial organization within cells. Here,…

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When you find in a Cell article figure the assay you used more than 20 years ago in your postdoc.... www.sciencedirect.com/science/arti...

That binding relates to activity, and activity should be the same on both leaflets. Unless cholesterol is not at equilibrium between the leaflets, as nothing in biology seems to be.

So, are you suggesting that the difference in cholesterol amounts between each leaflet is caused by protein binding? If so, does this relate to changes in cholesterol accessibility when toxins like Perfringolysin O bind to the membrane?

And the hydrolysis of the peptide bond is spontaneous…

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3/3 Hence, the use of the term "lipid raft" calls for a definition that is redundant given the already encompassing definition of lipid domains. #lipiddomain #membranes

2/3 Lipid domains appears when membranes phase separate. It is intuitive to understand that the properties of lipid domains will inevitably vary, based on the specific composition of the membrane in which they exist. #lipiddomain #membranes

#membranecomplexity #lipiddomain #lipidraft
1/3 Considering the intricate and diverse composition of biological membranes, any attempt to define lipid rafts merely adds confusion when compared with the simpler definition of lipid domains.