Theodicy: God's editing system for new protein (Introduction)

by David Turell , Wednesday, October 13, 2021, 19:09 (1135 days ago) @ David Turell

Cells contain chaperone molecules to monitor protein folding and correct or stop production:

https://www.sciencedaily.com/releases/2021/10/211012185717.htm

"The protein folding process, during which a chain of amino acids assumes its final shape as a protein, can be especially fraught. Researchers have long known that special molecules called chaperones help shepherd the protein into its final, correct shape. These "chaperones" can figure out which proteins are at risk of being deformed and can then lend that protein additional help. But how exactly they do their work has been poorly understood: "The chaperones do some kind of magic," says Alexandra Pozhidaeva, co-lead author of the paper

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"The trick is that, though there are tens of thousands of different proteins in our cells, each with a different shape and function, there are far fewer chaperones. "How is it," asks Lila Gierasch, Distinguished Professor of biochemistry and molecular biology at UMass Amherst and the paper's senior author, "that the same chaperones can help many different proteins?" The answer lies in what the authors call the chaperones' "selective promiscuity."

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"What they discovered is that Hsp70s are both promiscuous -- they can service many different proteins -- but also selective: the range of proteins they can work with is limited. Additionally, Hsp70s "read" ambidextrously: they can identify which protein chains to help by reading their sequences either from left to right, or right to left.

"Not only is this breakthrough an advance in our understanding of how cells stay healthy, it has real-world applications. "Hsp70s," says Gierasch, "are involved in so many pathological diseases, from cancer to Alzheimer's, and host Hsp70s are exploited by parasites and viruses. Understanding how Hsp70s work can help us develop therapeutic strategies against these terrible diseases.'"

Comment: Molecules don't think. Chaperone molecules are following protein formation and know when it is wrong. How they know based on protein reactions is yet to be discovered. When that is thoroughly researched, there will be automaticity, no thought involved, as in all other studies previously described..