How mechanical forces can modulate the metal affinity and selectivity of metal binding sites in proteins.

摘要: Mechanical forces play a key role in essential biological processes including cell growth, division, deformation, adhesion, migration and intra-cell interactions. The effect of mechanical modulating the structure properties metal-occupied protein binding sites has not been fully understood. Here, by employing combination density functional theory (DFT) calculations polarizable continuum model (PCM) computations applied on metal-loaded EF-hand sites, we shed light intimate mechanism Mg2+/Ca2+ competition impacted application stimuli. Applying force with specific directionality magnitude may shift balance between competing metal cations favor given contestant depending composition strength coordinative bonds robustness site. Furthermore, help to determine range rupture typical for these structures: from 0.4 1.5 nN nature amino acid residue. This positions Mg2+–O Ca2+–O that covalent hydrogen bonds. cation charged residue at higher (∼1.2–1.5 nN) relative those their metal–noncharged counterparts which dissociate ∼0.2–0.4 nN.