Green carbon

Fig. 6 Superimposition of inhibitors and key active site residues from crystal structures of oseltamivir carboxylate 18 brown carbons, PDB - 2qwk) and Neu5Ac2en 4 (green carbons, PDB - IfSb) in complex with influenza A virus siaMdase. Note the alternative conformations of the...

Fig. 5.16 Calculated structure of ferrous nitrosyl tetraphenylporphyrin Fe(TPP)(NO), resulting from geometric optimization with the B3LYP functional and 6-3IG -I- VTZ basis set [101]. Color scheme cyan = iron, green = carbon, blue = nitrogen, red = oxygen (taken from [101])...

Fig. 3 The SAR by NMR approach. Example of a small bidentate molecule designed using this approach. The example shown is for the design of a potent inhibitors of the matrix metalloproteinase MMP3. (a) Docked structures of the identified fragment leads are shown with cyan carbons, whereas the linked compound is shown with green carbon atoms. All structures were experimentally determined by NMR. (b) Chemical structures (and in vitro potencies) of the fragment leads and subsequent high-affinity linked compounds. Adapted from [7]...

Fig. 14.1. Ribbon structure (magenta) of the phosphorylase kinase crystal structure 2PHK (20) bound with ATP (green carbons, colored by atom type) and substrate peptide (light blue ribbon). The N- and C-terminal lobes are highlighted the hinge region is shown in cyan, the a-C helix in gray, and the -loop in orange.

Fig. 6 Details of active site alignment with unrefined DTX/ltub model with orange carbons and PTX/maidl with green carbons. Structure based site residue numbering from ltub (Nogales 1999), parenthetical numbering is based upon sequence and used in the text...

Fig. 23 Bridging biological space. The overlap of epothilone B (cyan carbons) and PTX (green carbons) models derived from EC reveal shared anchors between the exchangeable nucleotide site through H227 and the truncated B9-B10 loop of the beta tubulin site. Perhaps rigidifying this vector across the site is of greater importance to the MT stabilizing effect than picking up interactions within the deep hydrophobic pocket...

Figure S.8 Stereo view showing positions 60, 72, 104 and 117 in IFABP that have been used for the attachment of pyridoxamine and other catalytic groups. From top to bottom A104, Y117, L72 and V60. Color scheme Protein secondary structure (green), carbon (white), oxygen (red), nitrogen (blue).

Green carbon bodies were prepared by molding (rod 2x2x8 cm3) and by extrusion (rod 2 cm dia, and 11 cm length) from a mixture of appropriately sized calcined coke and coal tar binder pitch. The rods were then baked at a slow rate to 1,000°C in an electric furnace and kept at this temperature for an hour. The extruded rods were further graphitized at 2,800°C for 0,5 hr. under an argon flow. 

As an example, consider ethanol (right). The red carbon attached to the OH group will have relatively fewer electrons around it compared to the green carbon since the oxygen atom is more electronegative and draws electrons towards it, away from the carbon atom. 

At first glance, it is not at all clear that steroids are terpenoid in origin. The 5n numbers are absent— cholesterol is a C27 compound while the others variously have 20,21, or 23 carbon atoms. Studies with labelled mevalonic acid showed that cholesterol is terpenoid, and that it is formed from two molecules of farnesyl pyrophosphate (2 x C45 = C30 so three carbon atoms must be lost). Labelling of one or other of the methyl groups (two experiments combined in one diagram ) showed that two of the green carbon atoms and one of the black carbon atoms were lost during the biosynthesis. 

M. Brookhart, and M. L. H. Green, Carbon-Hydrogen-Transition Metal Bonds,... 

Figure 4.5 Assignment of atom types for the N and O atoms in Gin sidechains can be difficult and often relies on interpreting the H-bond partners in the local environment. For the two elastase structures lela (green carbon atoms) and lelc (yellow carbon atoms), a donor and an acceptor group in the ligand form close contacts with the Gin amide group, respectively. This allows unambiguous assignment of the O and N atom types. The position and orientation of the amide plane are almost identical in the two structures only the O and N positions are switched. The figure was prepared using RasMol [147].

Adsorption of carbon monoxide on a gallium-doped sample [NiO(10 Ga)(250°)] precovered by oxygen decreases the electrical conductivity of the solid, whose color changes from black to green. Carbon dioxide is therefore formed. It appears from cycles 1 and 2 (Table XIII) that the interaction product remains adsorbed on the most active surface sites (6 = 0) and is desorbed from less active sites (6 = J0m)-Carbon dioxide is indeed found in the cold trap (1 cm /gm). Since cycle 3 (Table XIV) is balanced neither for 0 = 0 nor for 0 = 0m, the intermediate formation of C03-(ads) is precluded. 

Phthalocyanine Blue Phthalocyanine Green Carbon Black. 

Fig. 10.6 S urfaces of the putative active sites of human FKBP12 (1 FKF) and human Pinl (1 PI N1) liganded to the inhibitors FK506 and Ala-Pro, respectively. Inhibitors are depicted as red stick models. Protein surfaces are shown in green, carbon red, oxygen blue, nitrogen. Coloration is in pale blue for the...

As soon as one comes across a green copper roof , one should attempt to remove the green layer until one reaches the pure red-brown copper metal. If one dissolves the green substance in diluted hydrochloric acid, bubbles form. The addition of limewater helps to prove the existence of carbon dioxide. The green substance must be a type of copper carbonate, a completely different substance than the red-brown metal. The formation of green carbonate can be explained by reactions of copper with the solution of carbon dioxide in rainwater, or the formation of blue copper sulfate by the reaction of copper with industrial acidic rain . 

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