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However, as we observe BSA denaturation with CD spectroscopy and binding to a scavenger receptor known to bind disrupted BSA, it is likely that protein disruption, rather than altered epitope exposure, is the main reason for the binding of BSA NP complexes formed from cationic NPs to scavenger receptors.
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The reason for which the binding site size of SSB changed, followed by swapping of the C-terminal domain, remains unclear.
It was observed that Δ Eele, Δ Evdw and Δ GSA were the main driving forces for inhibitor binding, whereas the net electrostatic contribution (Δ Eele+Δ GGB) difference was the leading reason for distinguishing the binding affinities of these two inhibitors.
This is the reason for the heterogeneous binding time and MSD in Fig. 8.
This backbone atom is also present in alanine, which may be the reason for the unchanged binding of the S346A mutant.
Conversely, the absence of specific polar interactions between the (R -enantiomers and AR -enantiomerso be the mand reArgB263r the different binding affinitieseemserved betoeen the two enantiomers.
A putative reason for the weak binding of hPS in the P1 site is the remoteness of the positively charged protein side chains from the site.
The reason for the slow binding is unknown.
This phenomenon may be the reason for the comparable binding affinities of PriB to ssDNA and dsDNA.
Given that C2F lipid membrane interaction is calcium-independent, the exact reason for the calcium binding activity of this domain is unclear.
The reason for the better binding with siRNA for NF51, PF6, and PF3, as compared to TP10, would appear to be the stearyl tail present in the former three, but lacking in TP10.
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