Titration binding isotherms

Figure 7.21 Experimental titration binding isotherms, (a) Hyperbolic titration binding isotherm...

Figure 13.10 Calorimetric titration response showing the exothermic raw (downward-projecting peaks, upper panel) heats of the binding reaction over a series of injections titrating 0.061 mM RNase A (sample) with 2.13 mM 2CMP at 30°C. Bottom panel shows the binding isotherm obtained by plotting the areas under the peaks in the upper panel against the molar ratio of titrant added. The thermodynamic parameters were estimated (shown in the inlay of the upper panel) from a fit of the binding isotherm.

Figure 4.32. Binding isotherms (a) and titration curves (b), and the corresponding slopes of and 6, for values of the binding constants calculated for the racemic form with k values from Table 4.8 (here, L is the trans form and H the cis-gauche form). Note the four peaks in the slope curves, corresponding to the four binding constants lo 2C be binding isotherms are plotted in...

G. THE RELATION BETWEEN THE BINDING ISOTHERM AND THE TITRATION CURVE FOR TWO-SITE SYSTEMS... 

In Section 2.6 we derived a relation between the binding isotherm 0 = ([FT]) and the titration curve Ng = N [H ), where [Ff is the proton concentration. This relation, for the one-site system, is... 

Figure G. 1. The titration curve (dashed line), and the binding isotherm (full line) (2 - 20) for a - a di-tert-butyl succinic acid (in 50% ethanol solution) pAj j = 3.58, = 13.12, and...

Fig. 1. (a) Raw calorimetric data obtained by the titration of 0.57 mM cysteine with 1.59 nM gold nanorod solution and (b) binding isotherm plot obtained by integrating each peak in raw data and normalizing with cysteine concentration. 

Fig. 9.3. Cu(ll)-binding isotherms for the resins (a) SDS as a co-surfactant, 0.5 g. (b) SDS, 1.0 g. Open circles, non-imprinted resin solid circles, Cu(Il)-imprinted resin solid triangles, Zn(II)-imprinted resin solid squares, Cd(II)-imprinted resin. Conditions 0.5 g of resin and Ckno.i = 0.1 mM, at 25°C for a potentiometric titration.

XH NMR experiments show that the viologen residue interacts effectively with the CB7 host [53], Voltammetric and mass spectrometric data are also consistent with the formation of inclusion complexes between the dendronized viologens and CB7. As was the case with methylviologen, complexation by CB7 depresses the molar absorptivity coefficient for the viologen UV absorption band and this effect can be conveniently utilized to fit the absorbance data in titration experiments to 1 1 binding isotherms. From the optimization of these fittings we obtained the corresponding equilibrium association constants (Table 3). 

Fig. 17.18 Characterization of GTP Green (a) absorption spectrum in MeOH (b)excitation and emission spectra in MeOH (c) fluorescence emission spectra (excitation = 480nm)of G49 with 100pM of GTP, ATP, all other 14 analytes and blank control in lOmM HEPES buffer (pH = 7.4) (d) fluorescence emission spectra (excitation 480nm, cutoff 495nm) of G49 with 500, 100, 50, 20, 12, lOpM GTP and blank control in lOmM HEPES buffer (pH = 7.4) (e) binding isotherm from the fluorescence titration experiment with emission at 540nm (f) picture of G49 with analytes under 365 nm UV lamp light...

Figure 3. Simulation of the kinetic scheme from Figure 2 using the constants from Table 3. The top figure represents the kinetics of Ca dissociation which has a biphasic response (fast phase 663 s and slow phase 9 s ). The middle figure represents the titration of calmodulin by Ca ". The signal rising between 0 and 2-3 Ca " ions is associated with the occupancy of the sites from the COOH terminus and the other signal is associated with the occupancy of the N-terminal sites. The bottom figure is a Scatchard representation of the direct calcium binding isotherm.

Figure 7.36 Peptide association with GroEL (a) Fluorescence emission spectra from fluorescence binding titration experiment with fixed concentration of AMPH+ peptide(0.5 / M) titrated with GroEL until saturation in buffer pH 7.5 at 20°C. Note blue shift and increase in emission intensity as titration progresses. (b) Three binding isotherms from three fluorescence binding titration experiments involving the indicated peptides under conditions described in (a) (Reproduced from Preuss et al., 1999, Fig. 6).

Figure 2. Raw isothermal titration calorimetry (top) and binding isotherm data (bottom) for the binding of Heml5 to apo (A) and holo (B) Yfhl. Data were collected by injecting small aliquots of a 550 juM Heml5 into a 50 pM Yfhl solution. Spacing between injections was 10 at a 500 rpm stirring speed.

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