Sandbox Reserved 960: Difference between revisions
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=== pH influence === | === pH influence === | ||
pH affects the flexibility of ASP1 because it induces a different protonation state of the <scene name='60/604479/Ionizable_residues/1'>ionizable residues</scene>. Protonated residues | pH affects the flexibility of ASP1 because it induces a different protonation state of the <scene name='60/604479/Ionizable_residues/1'>ionizable residues</scene>. Protonated residues give rise to micro-environnment changes which propagate all along the protein. Consequently, ASP1 is no longer able to interact with its ligands even if ionizable residues are distant from the cavity. <ref>PMID: 19481550</ref> | ||
In fact, depending of the pH level, Asp35 bend the C terminal domain against the cavity. | In fact, depending of the pH level, Asp35 bend the C terminal domain against the cavity. | ||
At pH 5.5, <scene name='60/604479/C-term_asp35/1'>Asp 35</scene> is protonated and C terminal domain isn’t bend against the cavity. While ASP1 is a monomere at acid pH, it can dimerize at neutral and basic pH.<ref>PMID: 25337796</ref> | At pH 5.5, <scene name='60/604479/C-term_asp35/1'>Asp 35</scene> is protonated and C terminal domain isn’t bend against the cavity. While ASP1 is a monomere at acid pH, it can dimerize at neutral and basic pH.<ref>PMID: 25337796</ref> | ||
