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In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1). Ion pairing is one of the most important noncovalent forces in chemistry, in biological systems, in different materials and in many applications such as ion pair chromatography .
In electrochemistry, a salt bridge or ion bridge is an essential laboratory device discovered over 100 years ago. [ 1 ] It contains an electrolyte solution, typically an inert solution, used to connect the oxidation and reduction half-cells of a galvanic cell (voltaic cell), a type of electrochemical cell .
Example salt bridge network in 2-deoxyribose-5-phosphate aldolase ( ). Interactions are shown as cyan dashed lines. Polar residues are colored green. Polar amino acids aspartate (D), glutamate (E), lysine (K), and arginine (R), are shown here. Salt bridges within TIM barrel pores are thought to contribute to the overall stability of the fold.
A chaotrope denatures biomolecules by disrupting the shell of hydration around them. This allows positively charged ions to form a salt bridge between the negatively charged silica and the negatively charged DNA backbone in high salt concentration. The DNA can then be washed with high salt and ethanol, and ultimately eluted with low salt.
Conserved residues in the linker between the two eIF4AIII domains form salt bridges or hydrogen bonds with specific residues in Magoh. [21] Other bonding occurs between the second loop of the Magoh β–sheet and the two eIF4AIII domains and their linker. [21] There is only a single partial bond formed between Y14 and eIF4AIII.
Bonding energies are significant, with solution-phase values falling within the same order of magnitude as hydrogen bonds and salt bridges. Similar to these other non-covalent bonds, cation–π interactions play an important role in nature, particularly in protein structure, molecular recognition and enzyme catalysis. The effect has also been ...
These anionic residues can interact with cationic residues such as lysine and arginine to form salt bridges, stable non-covalent interactions that alter a protein's structure. These phosphosites often participate in salt bridges, suggesting that some phosphorylation sites evolved as conditional "on" switches for salt bridges, allowing these ...
Other mechanisms include minimization of solvent accessibility of acidic residues or binding of metal cofactors. In a specialized case of acid stability, the NAPase protein from Nocardiopsis alba was shown to have relocated acid-sensitive salt bridges away from regions that play an important role in the unfolding process. In this case of ...