Sentence examples for binding sites with nm from inspiring English sources

We present a method for simultaneously recording topography images and localizing specific binding sites with nm positional accuracy by combining dynamic force microscopy with single molecule recognition force spectroscopy.

Scatchard analysis predicted for a single class of binding sites with Kd=1.4 nM.

Saturation binding in the hippocampus (one Alzheimer brain) revealed two binding sites, with Kd values of 3.1 nM and 34 nM and Bmax values of 250 fmol/mg and 1226 fmol/mg, respectively (Additional file 2).

EBNA1 DNA binding domain was purified to near homogeneity and capable of binding a fluorescent tagged DNA hairpin containing a consensus EBNA1 binding site with ∼50 nM affinity (data not shown).

Binding data from membrane preparations indicated the presence of two classes of binding sites with KD of 1.5 +/- 0.4 nM and 25.5 +/- 11.0 nM.

Additionally, competition binding experiments on human skin sections revealed that resveratrol competed for 50% of specific [3H]-resveratrol (30 nM) binding sites with a Ki value of 2.6±0.7 and 1.5±0.6 µM in the epidermis and dermis, respectively, which are highly similar to low affinity sites observed in brain homogenates (Fig. 3; see also [21]).

Data analysis according to a multiple stepwise equilibrium model using six constants reveals the presence of three high affinity binding sites with Kd values from 22-28 nM at 37°C (11), whereas analysis of the same data according to a single site equilibrium binding constant gives a Kd of 1.63 μM (12).

Accordingly, dimeric NOS has two identical binding sites with very high affinity for BH4 (≤1 nM), but binding of BH4 to one site lowers the affinity of the second site by several orders of magnitude.

Saturation isotherms fit a model of two independent binding sites with dissociation constants of 11 and 570 nM and corresponding densities of 2.5 and 47 pmol/mg protein.

CT-26 tumor cells showed specific saturable binding sites with a Kd of 35.09 ± 7.45 nM and a Bmax of 0.920 ± 0.077 pmol/million cells.

Palonosetron exhibited a concentration-dependent decrease in binding sites with an IC50 of 0.38 ± 0.02 nM, indicating that down-regulation occurs within a concentration range very similar to that of competition binding (dose ratio of 1.7 between the two measurements).