Ionic interaction in the context of Electronegativities

Ionic interaction in the context of Electronegativities

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⭐ Core Definition: Ionic interaction

Ionic bonding is a type of chemical bonding that involves the electrostatic attraction between oppositely charged ions, or between two atoms with sharply different electronegativities, and is the primary interaction occurring in ionic compounds. It is one of the main types of bonding, along with covalent bonding and metallic bonding. Ions are atoms (or groups of atoms) with an electrostatic charge. Atoms that gain electrons make negatively charged ions (called anions). Atoms that lose electrons make positively charged ions (called cations). This transfer of electrons is known as electrovalence in contrast to covalence. In the simplest case, the cation is a metal atom and the anion is a nonmetal atom, but these ions can be more complex, e.g. polyatomic ions like NH
4 or SO
4. In simpler words, an ionic bond results from the transfer of electrons from a metal to a non-metal to obtain a full valence shell for both atoms.

Clean ionic bonding – in which one atom or molecule completely transfers an electron to another – cannot exist: all ionic compounds have some degree of covalent bonding or electron sharing. Thus, the term "ionic bonding" is given when the ionic character is greater than the covalent character – that is, a bond in which there is a large difference in electronegativity between the cation and anion, causing the bonding to be more polar (ionic) than in covalent bonding where electrons are shared more equally. Bonds with partially ionic and partially covalent characters are called polar covalent bonds.

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Ionic interaction in the context of Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo-electron microscopy (cryo-EM) and dual polarisation interferometry, to determine the structure of proteins.

Protein structures range in size from tens to several thousand amino acids. By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.

View the full Wikipedia page for Protein structure
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LINKED FROM (PARENTS)
← Protein structure
LINKS TO (CHILDREN)
Sodium → Fluorine → Redox → Electron → Electron configuration → Exothermic → Sodium fluoride → Chemical bond → Coulomb's law → Ion → Atom → Electronegativities → Ionic compound → Covalent bond → Metallic bonding → Anion → Cations → Metal → Nonmetal → Polyatomic ion → Electronegativity → Polar covalent bond →