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It is well known that the donor binding energy has a peak as the QW width increases.
The binding energy has a maximum value when the impurity is located on the center of dots and decreases for other impurity positions.
It is clear from Table 10 that the total energy has a negative value, whereas the binding energy has a positive value (Table 7).
For F=0 the binding energy has a maximum value when the impurity is located at the center of the inner dot.
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From Table 3, when TP5 bound to the mutant DR11, the binding energy had a slight change; however, Ala11 completely lost its role as a binding site.
Whereas, when TP5 bound to the mutant DR62, the binding energy had a distinct change; Ala62 remained to exert a positive role as a binding site, suggesting that Asn anchor mainly contributed to the binding energy.
In fact, because a significant part of the binding energy has to be spent to fold a flexible protein, lack of structure and flexibility in the unbound state provide interactions with a mechanism to have both high specificity and low affinity, with the low affinity providing the basis for easy reversibility.
Also, the binding energy has two weaker symmetric local maxima for the impurity in the outer dots.
The results clearly showed that the binding energy has three peaks, that are around the center of dots, and decreases as the dot size increases.
However, kcat/KM is higher with both substrates for the triple mutant, indicating that binding energy has been diverted from substrate binding to transition state stabilization.
Dimerization or protein protein binding energy has been shown to be directly related to the buried hydrophobic surface area (Janin et al, 1988).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com