Cargando…
Diselenide crosslinks for enhanced and simplified oxidative protein folding
The in vitro oxidative folding of proteins has been studied for over sixty years, providing critical insight into protein folding mechanisms. Hirudin, the most potent natural inhibitor of thrombin, is a 65-residue protein with three disulfide bonds, and is viewed as a folding model for a wide range...
Autores principales: | Mousa, Reem, Hidmi, Taghreed, Pomyalov, Sergei, Lansky, Shifra, Khouri, Lareen, Shalev, Deborah E., Shoham, Gil, Metanis, Norman |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9814483/ https://www.ncbi.nlm.nih.gov/pubmed/36697775 http://dx.doi.org/10.1038/s42004-021-00463-9 |
Ejemplares similares
-
BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path
por: Mousa, Reem, et al.
Publicado: (2018) -
Harnessing selenocysteine reactivity for oxidative protein folding
por: Metanis, Norman, et al.
Publicado: (2015) -
One‐Pot Chemical Protein Synthesis Utilizing Fmoc‐Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F
por: Zhao, Zhenguang, et al.
Publicado: (2022) -
Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase
por: Lansky, Shifra, et al.
Publicado: (2022) -
Novel AIEgen-Functionalized Diselenide-Crosslinked Polymer Gels as Fluorescent Probes and Drug Release Carriers
por: Zhao, Jie, et al.
Publicado: (2020)