Molecular modeling reveals that disruption of a salt bridge between D474 and K445 accompanying with some H-bond deletion may be involved in destabilization of D474K mutant.
We show that disruption of a salt bridge, hydrogen bond network, and intermolecular van der Waals contacts between helices D and J in adjacent ligand binding cores greatly accelerates desensitization.
Glu237 of AQN corresponds to Gln230 of BgAP, and disruption of a salt bridge in E237Q resulted in a rapid decrease of activity during incubation at 70°C and 80°C.
Disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant resulted in a significant reduction in thermal stability, and a massive change in the content of the secondary structure was observed, even at 70°C, in the circular dichroism (CD) analysis.
The presence of this primate-specific K191 has been suggested to cause the disruption of a sulfhydryl bridge and subsequent formation of misfolded receptors resulting in the retention of the protein in the endoplasmic reticulum (ER) [11].
It has been reported that the molecular mechanism behind the 50% increase in N114S mutant enzyme activity is caused by a disruption of a salt bridge, which would otherwise stabilizes the dimer interface (Liu et al. 2009).
On the basis of these considerations, the 51 53 °C melting temperature of the D56S and R89N mutants is predicted to reflect disruption of a salt bridge and therefore a destabilization of the DNA binding lobe, leading to the inference that domain D1 (Tm ∼ 49 °C) in WT MftR corresponds to the dimer interface, while D2 (Tm ∼ 58 °C) represents the DNA binding region.
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The increased neddylation in the K472E/R473E Cul1 mutant, which leads to the disruption of a buried salt bridge in the four-helix bundomainmain of Cul1 [24], is likely a result of reduced binding of the deneddylating CSN complex (see Fig. 2b).
Recent results also show that a point mutation leading to the disruption of a single salt bridge in p53 increases propensity to form amyloid fibrils (Galea et al. 2005).
