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This canonical binding surface has been reported in several related literatures [18], [34], [35], [36], [37].
The core domain of RSV M2-1 has been reported to bind RNA with a 1 1 stoichiometry with significant preference for adenine rich sequences, and the binding surface has been located by NMR chemical shift perturbation experiments (Blondot et al., 2012).
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DOI: http://dx.doi.org/10.7554/eLife.10147.020 Why would a latent Pins binding surface have been present?
Adsorption of enzymes to the substrate during hydrolysis is desired because productive binding of proteins on the substrate surface has been shown to improve enzyme-substrate interactions.
The process of binding to bacterial receptors on the cell surface has been shown for several pathogens to be mediated by the PLG kringle domains through the lysine-binding sites present [20].
The surface binding forming for benzoic acid supported on TiO2 surface has been studied by the Fourier transform infrared spectroscopy.
Strong binding of the protein to the spicule silica surface has been attributed to this cluster (Müller et al. 2008a).
The road surface has been badly damaged.
DNA binding to cell-surfaces has been documented in several studies.
For example, reduced binding to polyanionic surfaces has been found with the 402H allele compared with 402Y (22, 22).
A new approach termed dPredGB to detect and evaluate putative binding cavities on protein surfaces has been developed.
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