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- W4321184666 endingPage "173" @default.
- W4321184666 startingPage "131" @default.
- W4321184666 abstract "There are many Archaea with flat, polygonal shapes, resembling shaped droplets in form. We hypothesized that the transition from abiogenesis to a living cell started with shaped droplets. We begin with proteins that have a transmembrane domain, such as the S layer, which is a common feature of Archaea and Bacteria. We show how the anchor transmembrane domain may have been hydrophobically “selected” from random mixed chirality peptides by the cell membrane itself when it was thinner, possibly produced from short meteorite amphiphiles. These peptides may have been the first proteins, formed mostly from three “core” amino acids that we deduce from t-RNA phylogeny: alanine, glycine, and isoleucine. They may have formed by PCR-like wet/dry cycles along with RNA, which may have protected them from hydrolysis as they grew, causing the membrane to thicken to its present thickness, a positive feedback, abiotic process. The possibly daily flattening and swelling of vesicles as the temperature changed at night, with 10 11 day/night cycles available, might have aided the PCR-like activity. Thus, the peptide/protein world may have been simultaneous with the RNA world. The juxtaposition of peptides with RNA may have led to the genetic code. Interactions between membrane-selected peptides and amphiphiles may have led to chirality of both." @default.
- W4321184666 created "2023-02-18" @default.
- W4321184666 creator A5032329081 @default.
- W4321184666 creator A5069542505 @default.
- W4321184666 date "2023-02-17" @default.
- W4321184666 modified "2023-10-17" @default.
- W4321184666 title "How to Make a Transmembrane Domain at the Origin of Life" @default.
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