ionic bond

(noun)

A strong chemical bond caused by the electrostatic attraction between two oppositely charged ions.

Related Terms

  • ion

Examples of ionic bond in the following topics:

  • Ions and Ionic Bonds

    • Ionic bonds are attractions between oppositely charged atoms or groups of atoms where electrons are donated and accepted.
    • Ionic bonds are formed between ions with opposite charges.
    • For instance, positively charged sodium ions and negatively charged chloride ions bond together to form sodium chloride, or table salt, a crystalline molecule with zero net charge.
    • In the formation of an ionic compound, metals lose electrons and nonmetals gain electrons to achieve an octet.
  • Hydrogen Bonding and Van der Waals Forces

    • Ionic and covalent bonds between elements require energy to break.
    • Ionic bonds are not as strong as covalent, which determines their behavior in biological systems.
    • However, not all bonds are ionic or covalent bonds.
    • Two weak bonds that occur frequently are hydrogen bonds and van der Waals interactions.
    • These bonds—along with ionic, covalent, and hydrogen bonds—contribute to the three-dimensional structure of proteins that is necessary for their proper function.
  • Water’s Solvent Properties

    • Water is therefore referred to as a solvent: a substance capable of dissolving other polar molecules and ionic compounds.
    • The charges associated with these molecules form hydrogen bonds with water, surrounding the particle with water molecules.
    • When ionic compounds are added to water, individual ions interact with the polar regions of the water molecules during the dissociation process, disrupting their ionic bonds.
    • Nonpolar molecules experience hydrophobic interactions in water: the water changes its hydrogen bonding patterns around the hydrophobic molecules to produce a cage-like structure called a clathrate.
    • This change in the hydrogen-bonding pattern of the water solvent causes the system's overall entropy to greatly decrease, as the molecules become more ordered than in liquid water.
  • Covalent Bonds and Other Bonds and Interactions

    • Its biosynthesis involves breaking the triple bond of molecular nitrogen, or N2, followed by the formation of several carbon-nitrogen single and double bonds.
    • These bonds are stronger and much more common than are ionic bonds in the molecules of living organisms.
    • Thus, triple bonds are the strongest.
    • Not all bonds are ionic or covalent; weaker bonds can also form between molecules.
    • Two types of weak bonds that frequently occur are hydrogen bonds and van der Waals interactions.
  • Protein Structure

    • Secondary structures arise as H bonds form between local groups of amino acids in a region of the polypeptide chain.
    • Enzymes often play key roles in bonding subunits to form the final, functioning protein.
    • For example, insulin is a ball-shaped, globular protein that contains both hydrogen bonds and disulfide bonds that hold its two polypeptide chains together.
    • Silk is a fibrous protein that results from hydrogen bonding between different β-pleated chains.
    • The tertiary structure of proteins is determined by hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages.
  • Control of Metabolism Through Enzyme Regulation

    • These molecules bind temporarily through ionic or hydrogen bonds or permanently through stronger covalent bonds.
  • The Periodic Table

    • Together they form an ionic compound, NaCl, or table salt, that is safely consumed by humans everyday.
    • As elements are bonded together they form compounds that often have new emergent properties that are different from the properties of the individual elements.
  • Peptide Bonding between Amino Acids

    • The peptide bond is an amide bond which links amino acids together to form proteins.
    • The bond that holds together the two amino acids is a peptide bond, or a covalent chemical bond between two compounds (in this case, two amino acids).
    • The amide bond can only be broken by amide hydrolysis, where the bonds are cleaved with the addition of a water molecule.
    • The peptide bond (circled) links two amino acids together.
    • Peptide bonds are amide bonds, characterized by the presence of a carbonyl group attached to an amine.
  • Organic Isomers

    • Structural isomers (such as butane and isobutane ) differ in the placement of their covalent bonds.
    • Geometric isomers, on the other hand, have similar placements of their covalent bonds but differ in how these bonds are made to the surrounding atoms, especially in carbon-to-carbon double bonds.
    • When the carbons are bound on the same side of the double bond, this is the cis configuration; if they are on opposite sides of the double bond, it is a trans configuration.
    • Fats with at least one double bond between carbon atoms are unsaturated fats.
    • (b) Geometric isomers have a different arrangement of atoms around a double bond.
  • Hydrocarbons

    • Furthermore, individual carbon-to-carbon bonds may be single, double, or triple covalent bonds; each type of bond affects the geometry of the molecule in a specific way.
    • Double and triple bonds change the geometry of the molecule: single bonds allow rotation along the axis of the bond, whereas double bonds lead to a planar configuration and triple bonds to a linear one.
    • When carbon forms single bonds with other atoms, the shape is tetrahedral.
    • When two carbon atoms form a double bond, the shape is planar, or flat.
    • Single bonds, like those found in ethane, are able to rotate.
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