Design and <i>Escherichia coli</i> Expression of a Natively Folded Multi-Disulfide Bonded Influenza H1N1-PR8 Receptor-Binding Domain (RBD)

Design and <i>Escherichia coli</i> Expression of a Natively Folded Multi-Disulfide Bonded Influenza H1N1-PR8 Receptor-Binding Domain (RBD)

Refolding multi-disulfide bonded proteins expressed in <i>E. coli</i> into their native structure is challenging. Nevertheless, because of its cost-effectiveness, handiness, and versatility, the <i>E. coli</i> expression of viral envelope proteins, such as the RBD (Receptor-B...

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Bibliographic Details
Main Authors: Thao Tu, Tharangani Rathnayaka, Toshiyo Kato, Kenji Mizutani, Tomonori Saotome, Keiichi Noguchi, Shun-ichi Kidokoro, Yutaka Kuroda
Format: Article
Language:English
Published: MDPI AG 2024-04-01
Series:International Journal of Molecular Sciences
Subjects:
influenza A
H1N1
receptor-binding domain
refolding
NMR
<i>E. coli</i> expression system
Online Access:https://www.mdpi.com/1422-0067/25/7/3943

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