Electron density difference plot from

Fig. 2.9. Electron density difference plots for a Pd atom bound at a regular 0 site (top) and at anF center (bottom). Ap = p(Pd/MgO)—/o(Pd)—/o(MgO). Reproduced from [64]. Copyright 2001 American Institute of Physics...

In an earlier investigation of silicon and copper [10, 11], Gorokhov and one of the present authors demonstrated that the potential curves for various types of bond differed more strongly than the electron density distributions plotted from the same experimental values of Fj. In view of this, it seemed desirable to repeat the earlier investigations of lithium fluoride to obtain the potential distribution in its lattice. 

Different depictions of the 2 s orbital, (a) A plot of electron density vs. distance from the nucleus, (b) An... 

Fig. 7.57 Plot of the isomer shift 5 of the 36.2 keV Mdssbauer transition of Os versus Dirac-Fock values for the electron density differences at the Os nuclei in free ion 5d configurations. The numbers of the data points refer to the numbering of the compounds in Table 7.9 (from [258])...

Figure 2.25. Charge density difference plot of N2 adsorbed on Ni(100). Regions of electron loss are indicated with dashed outer line and increase with full line. We have chosen a plane containing the interacting metal atom with one N2 molecule in the same plane. From Ref. [3].

To illustrate the magnitude of relativistic effects — kinematic as well as spin-orbit effects — electron density differences are depicted in Figure 16.4 for Ni(C2H2) and Pt(C2H2). For these plots various approximate electron densities have been subtracted from the four-component reference result. 

Figure 11 Electron density difference (EDD) plots for the reactant (top) and transition state (bottom). Dotted contours represent regions where electron density is depleted, whereas solid curves indicate where there is a gain in electron density on transferring the solute from the gas phase into water. The reactant is 3

Fig. 2.3 Electron density contour plot of HC = N superimposed to its gradient vector field, which consists of an infinite multitude of gradient paths, here represented by a few dozen paths originating at infinity and terminating at the respective nuclei. A special bundle of gradient paths starts at infinity and ends up at the little squares, which are bond critical points. From each bond critical point emerge two gradient paths, each of which is attracted to a different nucleus. This pair of gradient paths is called the atomic interaction line, or in this case of a local ena-gy minimum, the bond path. The carbon is placed at the origin and the bold square box marks the -6 a.u. and +6 a.u. horizontal and vertical boundaries of the plot. The electron density values of the contour lines are 1 X 10 , 2 X 10 , 4 X 10 and 8 x 10 " au where n starts at -3 and increases with unity increments...

Using the combination of main-frame CDC 6400 and Tektronix computations, a number of phenomena were studied with electron density functions, and especially with projection plots. Particularly useful were plots of difference functions in which the electron distributions of isoelectronic systems were compared directly. In such applications, we noted that a corresponding difference plot of the electron density itself in any given plane is not meaningful since the number of electrons may change that is, from one compound to the next the electron density can shift from one plane to elsewhere. In the projection plot the total number of electrons remains the same for both species and the integral of an isoelectronic difference function must sum to zero. Some examples of the kinds of problems studied are the vm transition of formaldehyde, substituent effects in substituted benzenes, and polarization... 

Figure 8.3 The DNA-binding protein Cro from bacteriophage lambda contains 66 amino acid residues that fold into three a helices and three P strands, (a) A plot of the Ca positions of the first 62 residues of the polypeptide chain. The four C-terminal residues are not visible in the electron density map. (b) A schematic diagram of the subunit structure. a helices 2 and 3 that form the helix-turn-helix motif ate colored blue and red, respectively. The view is different from that in (a), [(a) Adapted from W.F. Anderson et al., Nature 290 754-758, 1981. (b) Adapted from D. Ohlendorf et al., /. Mol. Biol. 169 757-769, 1983.]...

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