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A possible initial folding intermediate: the C-terminal proteolytic domain of tryptophan synthase beta chains folds in less than 4 milliseconds into a condensed state with non-native-like secondary structure.
Chaffotte AF, Cadieux C, Guillou Y, Goldberg ME. Chaffotte AF, et al. Biochemistry. 1992 May 5;31(17):4303-8. doi: 10.1021/bi00132a022. Biochemistry. 1992. PMID: 1567876
However, this state has non-native-like secondary and supersecondary structures [Chaffotte, A., Guillou, Y., Delepierre, M., Hinz, H.-J., & Goldberg, M. E. (1991) Biochemistry 30, 8067-8074]. ...These observations strongly suggest that the previously described c …
However, this state has non-native-like secondary and supersecondary structures [Chaffotte, A., Guillou, Y., Delepierre, M., H …
From transglutaminases (TGs) to arylamine N-acetyltransferases (NATs): Insight into the role of a spatially conserved aromatic amino acid position in the active site of these two families of enzymes.
Xu X, Zhang W, Berthelet J, Liu R, Michail C, Chaffotte AF, Dupret JM, Rodrigues-Lima F. Xu X, et al. Among authors: chaffotte af. Biochem Biophys Res Commun. 2020 Apr 30;525(2):308-312. doi: 10.1016/j.bbrc.2020.02.082. Epub 2020 Feb 20. Biochem Biophys Res Commun. 2020. PMID: 32089267
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