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The current study is the first to extend the SHCS technique to detection and investigation of protein binding at a surface.
Compounds were then developed and were shown to block the binding of an α-helix peptide from FtsZ.[ 15] Fesik and colleagues recently used a fragment-based approach to develop small molecules that prevent Sos binding to K-Ras by binding at a surface site of K-Ras.[ 16] Despite these successes, identification of fragments at PPI sites is not always possible.
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For the reversible binding of molecules at a surface, these dynamic processes can include diffusion in and out of the observation volume and absorption and desorption of the molecules to the surface.
During DNA translocation, the nuclease domain was proposed to interact with DNA through electrostatic interactions at a second DNA-binding site located at a surface opposite to the nuclease active site.
Therefore this layer is likely due to strong CBM binding at the surface along with an inherent property of the Cel9A CD that inhibits its penetration (e. g. larger size that slows its entry into the bulk of the film).
As we observed with the serotype D strains, the serotype A isolates examined also displayed plasminogen binding at the surface (Fig. 1B).
Availability of biotin for streptavidin binding at the surface of the fibers has been determined via a competitive colorimetric assay.
Interatomic binding at the surface is determined by both ionic and covalent contributions with a clear distinction between terminal oxygens and different bridging surface oxygens.
In this review article, we discuss a class of biosensors that exploit the change in the colorimetric properties of noble metal nanoparticles in response to biomolecular binding at their surface.
All of the investigated ligands listed in Table 1 were found to undergo binding at the surface (see inset in Fig. 1), inducing new hybrid properties of the surface-modified nanoparticle colloids.
However, in the absence of this cation no protein fluorescence was detected at surface pressures ≥30 mN/m, which is consistent with protein exclusion from the interface or less protein binding at such surface pressures in the absence of calcium.
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