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  2. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    In organic chemistry, covalent bonding is much more common than ionic bonding. Covalent bonding also includes many kinds of interactions, including σ-bonding, π-bonding, metal-to-metal bonding, agostic interactions, bent bonds, three-center two-electron bonds and three-center four-electron bonds. [2] [3] The term covalent bond dates from 1939 ...

  3. Bioorganometallic chemistry - Wikipedia

    en.wikipedia.org/wiki/Bioorganometallic_chemistry

    Bioorganometallic chemistry is the study of biologically active molecules that contain carbon directly bonded to metals or metalloids. The importance of main-group and transition-metal centers has long been recognized as important to the function of enzymes and other biomolecules.

  4. Chemical bond - Wikipedia

    en.wikipedia.org/wiki/Chemical_bond

    Molecules that are formed primarily from non-polar covalent bonds are often immiscible in water or other polar solvents, but much more soluble in non-polar solvents such as hexane. A polar covalent bond is a covalent bond with a significant ionic character. This means that the two shared electrons are closer to one of the atoms than the other ...

  5. Molecule - Wikipedia

    en.wikipedia.org/wiki/Molecule

    A covalent bond is a chemical bond that involves the sharing of electron pairs between atoms. These electron pairs are termed shared pairs or bonding pairs , and the stable balance of attractive and repulsive forces between atoms, when they share electrons, is termed covalent bonding .

  6. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Reversible covalent – a chemical bond is formed, however the free energy difference separating the noncovalently-bonded reactants from bonded product is near equilibrium and the activation barrier is relatively low such that the reverse reaction which cleaves the chemical bond easily occurs; Irreversible covalent – a chemical bond is formed ...

  7. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  8. Ligand (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Ligand_(biochemistry)

    Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of ligand in metalorganic and inorganic chemistry , in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin .

  9. Intramolecular force - Wikipedia

    en.wikipedia.org/wiki/Intramolecular_force

    In a true covalent bond, the electrons are shared evenly between the two atoms of the bond; there is little or no charge separation. Covalent bonds are generally formed between two nonmetals. There are several types of covalent bonds: in polar covalent bonds , electrons are more likely to be found around one of the two atoms, whereas in ...