ionic bond

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.