Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase.

Abstract

The three-dimensional crystal structure of the glycosyl phosphatidylinositol (GPI)-modified form of Torpedo acetylcholinesterase reveals the participation of Arg-44 and Glu-92 in a salt bridge and a hydrogen bond between Asp-93 and Tyr-96. To investigate the biological significance of these interactions, we have made amino acid replacements in this form of… (More)

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Cite this paper

@article{Bucht1994ResiduesIF, title={Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase.}, author={G{\"o}sta Bucht and Bj{\"o}rn H{\"a}ggstr{\"o}m and Zoran Radic and A. Osterman and Kerstin Hjalmarsson}, journal={Biochimica et biophysica acta}, year={1994}, volume={1209 2}, pages={265-73} }