Bonding nature

The very low solubility of oxamide is almost undoubtedly the result of the extensively hydrogen-bonded nature of the crystalline compound (cf. E. M. Ayerst and J. R. C. Duke, Acta. Cryst. (1954), 7, 588). 

Some characteristic bonding natures in typical nonclassical ions are the following. 

The ability to bond natural rubber to itself and to steel makes it ideal for lining tanks. Many of the synthetic elastomers, while more chemically resistant than natural rubber, have veiy poor bonding characteristics and hence are not well suited for hning tanks. 

Matsumura, M., Signor, G., Matthews, B.W. Substantial increase of protein stability by multiple disulfide bonds. Nature 342 291-293, 1989. 

Azulene does have an appreciable dipole moment (0.8 The essentially single-bond nature of the shared bond indicates, however, that the conjugation is principally around the periphery of the molecule. Several MO calculations have been applied to azulene. At the MNDO and STO-3G levels, structures with considerable bond alternation are found as the minimum-energy structures. Calculations which include electron correlation effects give a delocalized n system as the minimum-energy structure. ... 

Why should the cores of most globular and membrane proteins consist almost entirely of a-helices and /3-sheets The reason is that the highly polar N—H and C=0 moieties of the peptide backbone must be neutralized in the hydrophobic core of the protein. The extensively H-bonded nature of a-helices and /3-sheets is ideal for this purpose, and these structures effectively stabilize the polar groups of the peptide backbone in the protein core. 

Metal-oxenoid (oxo metal) species and metal-nitrenoid (imino metal) species are isoelectronic and show similar reactivity both species can add to olefins and be inserted into C—H bonds. Naturally, the study of nitrene transfer reactions began with metalloporphyrins, which were originally used as the catalysts for oxene transfer reactions. 

Biosynthesis of the polypeptide chain is realised by a complicated process called translation. The basic polypeptide chain is subsequently chemically modified by the so-called posttranslational modifications. During this sequence of events the peptide chain can be cleaved by directed proteolysis, some of the amino acids can be covalently modified (hydroxylated, dehydrogenated, amidated, etc.) or different so-called prosthetic groups such as haem (haemoproteins), phosphate residues (phosphoproteins), metal ions (metal-loproteins) or (oligo)saccharide chains (glycoproteins) can be attached to the molecule by covalent bonds. Naturally, one protein molecule can be modified by more means. 

The orbital bonding nature within carbon nanotubes creates unique electrical properties within a non-metallic molecule, which is a result of the delocalization of the -electron donated by each atom. Electrical conductivity can take place along the entire nanotube due to the freedom of -electron flow, making possible the design of circuits of extremely low nanometer diameter. 

Such hydrophobic H-bonding naturally leads to an appreciable reduction in volume, and is therefore increasingly favored at higher pressures. Similarly, in the spirit of LeChatelier s principle, one may expect that the presence of a hydrophobic solute promotes formation of cage structures, i.e., tends to shift the cluster... 

It was confirmed that the change in the rc-bond lengths upon one-electron oxidation of 12-15 is systematically related to the coefficients of the relevant carbons HOMO of the neutral molecules. The bonds with the bonding nature in the HOMO of the neutral molecules are elongated upon reflioval of one electron, and those with antibonding nature in HOMO are shortened. 

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