Investigation of mutations to customize structurally dynamic papain proteins for temperature-specific peptide binding by complementary use of two different artificial intelligence methods and molecular simulations
Customization of proteins to undertake temperature-specific functions would expand their scope of use in medical treatment, food processing, and bioelectronic devices. To customize papain for temperature-specific peptide binding, the dynamic structure of papain was modified by repeatedly mutating V1...
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| Main Author: | Katsuhiko Nishiyama |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
AIP Publishing LLC
2025-03-01
|
| Series: | AIP Advances |
| Online Access: | http://dx.doi.org/10.1063/5.0216782 |
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