Syracuse University (Syracuse University) Ivan V. Korendovych and other researchers guided the directional evolution of protein by using nuclear magnetic resonance (Nuclear magnetic resonance (NMR)) , simplifying and efficient protein evolution process . In the experiment that proves the concept, the researchers evolved the enzyme-free myoglobin (myoglobin) (myoglobin) through only three mutations to an enzyme that is comparable to the enzyme related to natural-related enzymes (1).
The basic principle of of this method is: to produce or strengthen a certain catalytic function, its active site is near its active site, or other related positions at the distal end of (acting through allosteric effects, etc.) must require certain amino acid residues "reconstruction" , and this "reconstruction" can be monitored by NMR at the protein and its catalyzed substrate analog (usually a competitive inhibitor ) binds to the protein backbone site. Therefore, the next focus will be on the amino acid residues and their adjacent sites that have changed the chemical environment of (protein binding to its substrate analog) in this process and can efficiently evolve in a directional manner (1).
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Comment(s):
can also evolve against "non-structural areas". Although it is more difficult, it is also unique to this strategy.
In addition, combined with the large amount of protein conformation and catalytic function correlation data generated during the evolution of this strategy protein, it is expected to further analyze the molecular dynamics mechanism of enzyme catalyzing .
References:
1. S. Bhattacharya et al., NMR-guided directed evolution. Nature, 1–5 (2022).
Original link:
https://www.nature.com/articles/s41586-022-05278-9
