Journal:Protein Science:4: Difference between revisions
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Image:2024_Lushchekina_Prot_Sci_x.jpg| thumb |left|150px|For a divalent cation, it is hard to unbind from structural motifs composed of 4 acidic residues (4A). However, it is much easier if the motif is surrounded by 3 basic residues (4A/3B). [https://doi.org/10.1002/pro.5206 paper | <imagemap> | ||
Image:2024_Lushchekina_Prot_Sci_x.jpg| thumb |left|150px|For a divalent cation, it is hard to unbind from structural motifs composed of 4 acidic residues (4A). However, it is much easier if the motif is surrounded by 3 basic residues (4A/3B). defai;t [https://doi.org/10.1002/pro.5206 paper </imagemap> | |||
''Torpedo californica'' acetylcholinesterase (''Tc''AChE) contains a unique 4D motif composed of four aspartate residues that can bind divalent metal cations (like Ca²⁺, Mg²⁺, Mn²⁺), significantly increasing the enzyme’s thermal stability. Despite the electrostatic repulsion expected between these aspartates, structural analysis shows that the enzyme's conformation remains stable | ''Torpedo californica'' acetylcholinesterase (''Tc''AChE) contains a unique 4D motif composed of four aspartate residues that can bind divalent metal cations (like Ca²⁺, Mg²⁺, Mn²⁺), significantly increasing the enzyme’s thermal stability. Despite the electrostatic repulsion expected between these aspartates, structural analysis shows that the enzyme's conformation remains stable | ||
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