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Understanding the molecular origin of protein thermostability and thermoactivity attracted the interest of many scientists both for the perspective comprehension of the principles of protein structure and for the possible biotechnological applications through protein engineering.
Understanding of the molecular origin of protein thermostability and thermoactivity attracted the interest of many scientist both for the perspective comprehension of the principles of protein structure and for the possible biotechnological applications through application of protein engineering.
Antonio Lazcano also sympathized with the RNA world hypothesis and reviewed comprehensive evidence in its support, emphasizing on the catalytic properties of RNA (that is, ribozymes) and its evolutionary relevance for the origin of protein biosynthesis (for a historical recount leading to the formulation of the RNA world hypothesis see Lazcano 2012).
The surprising ability of RNA molecules to catalyze an increasingly large number of chemical reactions has lent strong support to the possibility of the so-called RNA world, and as discussed here with surprising clarity by Andrew Ellington, greatly simplifies the understanding of the origin of protein biosynthesis and of the genetic code.
The current study brings out three major lines of corroborating evidence for the random-sequence origin of protein coding split-genes.
To understand the origin of protein stability and cooperativity, we chose to examine a protein the folding of which is well characterized structurally, thermodynamically, and kinetically.
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"Proteogenesis" (the origin of proteins) is a likely key event in the unsolved problem of biogenesis (the origin of life).
If codons were assigned prebiotically, then the stop-codons were needed in the origin of protein-coding sequences.
The initial analysis based on the random-sequence origin of protein-coding genes [27], [30], [31] with limited data provided evidence that the DNA of eukaryotic organisms may be highly random.
Cells were isotopically labeled in culture using SILAC [23] to allow ascertainment of the cellular origin of proteins identified in media.
In some cases, this type of analysis could be informative as to the origin of proteins that have arisen through recombination or have been adapted to 'new' functions [70].
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