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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Bibliographic Details
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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