Salt bridges

spinqualitylabelsall models Salt bridge between retinoic acid(-) and arg131(+) in 1cbr. Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D In proteins, salt bridges occur between amino acid side-chains with opposite positive or negative full-electron charges, namely, (at neutral pH) Glu- or Asp- vs. Arg+ or Lys+. They may also occur between ionized organic ligands, such as acetylcholine+ (or example at right: 1cbr), or inorganic ions, such as K+ or SO4=, and amino acid side-chains. A salt bridge is generally considered to exist when the centers of charge are 4 Å or less apart. The center of charge of the arginine sidechain is the zeta carbon. The energetic significance of such complementary charge pairs is a complex function of the local environment. Proteins from thermophiles have more salt bridges than do proteins from mesophiles. These additional salt bridges contribute to stability, resisting denaturation by high temperature. Examples Thermophile vs. mesophile Glutamate dehydrogenase structures have been determined at about 2 Å resolution for both a thermophile, Pyrococcus furiosus (1gtm), and a mesophile, Clostridium symbiosum (1hrd). The thermophile's protein has 1.7 fold more N and O atoms engaged in salt bridges than does the protein from the mesophile (301 vs. 175 respectively, as counted by FirstGlance). Ultraviolet-B receptor UVR8 is an ultraviolet-B receptor in plants such as Arabidopsis. It is a homodimer that, upon irradiation, dissociates into a monomer involved in transcriptional activation of UV protective proteins. Unexpectedly, high ionic strength was found to dissociate the dimer. The homodimer 4dnw contains many salt bridges and cation-pi interactions at the interface. More.

Visualization

Putative protein-protein salt bridges involving charged amino acid sidechains and/or charged chain termini can be displayed by 1cbr.

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Eric Martz