Circular permutation at azurin’s active site slows down its folding
Author:
Funder
Department of Atomic Energy (DAE), India
Publisher
Springer Science and Business Media LLC
Subject
Inorganic Chemistry,Biochemistry
Link
https://link.springer.com/content/pdf/10.1007/s00775-023-02023-z.pdf
Reference74 articles.
1. Bliven S, Prlić A (2012) Circular Permutation in Proteins. PLoS Comput Biol 8:e1002445. https://doi.org/10.1371/journal.pcbi.1002445
2. Yu Y, Lutz S (2011) Circular permutation: a different way to engineer enzyme structure and function. Trends Biotechnol 29:18–25. https://doi.org/10.1016/j.tibtech.2010.10.004
3. Viguera AR, Serrano L, Wilmanns M (1996) Different folding transition states may result in the same native structure. Nat Struct Biol 3:874–880. https://doi.org/10.1038/nsb1096-874
4. Cellitti J, Llinas M, Echols N et al (2007) Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment. Protein Sci 16:842–851. https://doi.org/10.1110/ps.062628607
5. Chuang YC, Hu IC, Lyu PC, Hsu STD (2019) Untying a protein knot by circular permutation. J Mol Biol 431:857–863. https://doi.org/10.1016/j.jmb.2019.01.005
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