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- W2052803823 abstract "The secondary structure of the recently sequenced chicken liver cathepsin L (EC 3.4.22.15) has been studied both by circular dichroism and a predictive method. The structural data provided by these approaches allow us to underline the extent of the structural similarities between cathepsin L and papain, one of the best known proteins in the cysteine proteinase family. The predictive method of Garnier et al. (J. Mol. Biol. 120 (1978) 97–120) is used to locate α-helix and β-sheet segments in the cathepsin L sequence. An optimization of decision constants has been performed, using circular dichroism data, to improve good predictions. The combination of these approaches lead us to suggest that the location of ordered structures observed in papain is maintained in cathepsin L, but with an additional α-helix in the middle region (residues 85–108) of cathepsin L. Furthermore, we show that cathepsin L inactivation at neutral pH is correlated to the lost of α-helix content (40% at pH 5.8 and 17% at pH 7.0) in this protein. It appears that such an effect can be related to the change in the ionization state of histidine side-chains which are shown to be mainly located in the predicted α-helix regions." @default.
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- W2052803823 date "1988-06-01" @default.
- W2052803823 modified "2023-10-14" @default.
- W2052803823 title "Delineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content" @default.
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- W2052803823 doi "https://doi.org/10.1016/0167-4838(88)90179-3" @default.
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