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  2. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    The chemical energy released in the formation of non-covalent interactions is typically on the order of 1–5 kcal/mol (1000–5000 calories per 6.02 × 10 23 molecules). [2] Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects. [3] [2]

  3. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Irreversible covalent – a chemical bond is formed in which the product is thermodynamically much more stable than the reactants such that the reverse reaction does not take place. Bound molecules are sometimes called a "molecular complex"—the term generally refers to non-covalent associations. [2]

  4. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...

  5. 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 ...

  6. 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 .

  7. Bonding in solids - Wikipedia

    en.wikipedia.org/wiki/Bonding_in_solids

    As noted above, covalent and ionic bonds form a continuum between shared and transferred electrons; covalent and weak bonds form a continuum between shared and unshared electrons. In addition, molecules can be polar, or have polar groups, and the resulting regions of positive and negative charge can interact to produce electrostatic bonding ...

  8. Molecular recognition - Wikipedia

    en.wikipedia.org/wiki/Molecular_recognition

    The term molecular recognition refers to the specific interaction between two or more molecules through noncovalent bonding such as hydrogen bonding, metal coordination, hydrophobic forces, [3] [4] van der Waals forces, π-π interactions, halogen bonding, or resonant interaction [5] effects.

  9. 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 ...