Biological complexity: protein folding creates life (Introduction)

by David Turell , Sunday, July 17, 2022, 16:22 (860 days ago) @ David Turell

a new study of protein folding and form change creating a new function:

https://www.sciencedaily.com/releases/2022/07/220715142146.htm

"Though it has long been known that proteins wiggle and move, scientists have debated the significance of this "dancing" act, says Dominique Frueh, Ph.D., associate professor of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine. "The way proteins engage with the right partner at the right time -- essentially, how they communicate -- is very important for understanding their function," he says, "and we have found that protein wiggles are critical for this communication."

"In a bid to further such understanding, Frueh's team studied the wiggling action of the HMWP2 protein, a type of enzyme called nonribosomal peptide synthetases. These enzymes are made of several domains, or distinct regions, that work together like an assembly line to make complex natural products from small chemicals.

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"'We found that the two domains would only bind to one another as the second domain gets modified, which means they would only engage as needed for making the product and avoid wasting time together when the second domain is not modified," says Frueh. "Somehow, the first domain is able to sense when the second domain is modified, and we sought to investigate whether motions played a role in this recognition process."

"They also found changes in motion across the entire domain flagged with carbon-13c, not only where it binds to the second domain but also at a second, remote binding site used by a third domain.

"On an atomic level, Frueh says these two sites on HMWP2 could be considered "far" apart -- about 40 billionths of a meter. And how they interact, despite their distance, was particularly intriguing to the scientists.

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"'We found that the protein domain was structurally stable, but all of its movement was hindered," says Frueh. The mutated protein's lack of movement damaged its ability to bind with other domains even when they were modified, according to the researchers, demonstrating that the motions within the protein were necessary for the domains to work together."

Comment: we know that protein folding creates new functions, but how the proteins 'know' how to relate is still the very complex black box of functional proteins creating life. Only a designer mind can have created this.