Journal:Protein Science:4: Difference between revisions
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<br /><big>Lushchekina, Weiner, Ashani, Emrizal, Firdaus-Raih, Silman & Sussman</big><ref>PMID: 39548604</ref> | <br /><big>Lushchekina, Weiner, Ashani, Emrizal, Firdaus-Raih, Silman & Sussman</big><ref>PMID: 39548604</ref> | ||
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br>[[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 Go to paper] ]] | ||
[[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] ]] | |||
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