Biology › Definitions › Biological molecules, water and inorganic ions
Biological molecules, water and inorganic ions definitions
Every term defined in this unit, lesson by lesson, in the same words the lessons use, with a link to the notes where you will see it used.
Carbohydrate structure and function
- Monosaccharide
- A single sugar unit, the monomer from which disaccharides and polysaccharides are built.
- Monomer
- A small molecule from which a larger one is built by joining many of them together.
- Polymer
- A large molecule made of many similar monomers joined together.
- Macromolecule
- A very large molecule with a high relative molecular mass, such as a polysaccharide, a protein, a nucleic acid or a triglyceride.
- Condensation
- A reaction that joins two molecules with a covalent bond and releases a molecule of water.
- Hydrolysis
- A reaction that breaks a covalent bond between two molecules using a molecule of water.
- Glycosidic bond
- The covalent bond formed by condensation between two monosaccharides, joining them through an oxygen atom.
- Disaccharide
- Two monosaccharides joined by a glycosidic bond.
- Polysaccharide
- Many monosaccharides joined by glycosidic bonds into one large molecule.
- Tensile strength
- The greatest pulling force a material can withstand before it breaks, divided by its cross-sectional area.
- Retting
- Soaking or leaving plant stems in damp conditions so that microorganisms digest the pectins binding the fibres to the tissue around them, and the fibres can be separated.
- Sustainability
- Using resources to meet present needs in a way that does not reduce the ability of future generations to meet theirs.
- Biodegradable
- Able to be broken down by microorganisms into simple substances such as carbon dioxide and water.
- Polylactic acid
- A plastic made by fermenting glucose from plant starch into lactic acid and polymerising it; abbreviated to PLA.
Lipids: triglycerides, phospholipids and ester bonds
- Lipid
- A biological molecule that is largely non-polar, insoluble in water and soluble in organic solvents such as ethanol.
- Triglyceride
- One glycerol molecule joined to three fatty acids by three ester bonds.
- Ester bond
- The covalent bond formed by condensation between a hydroxyl group of glycerol and the carboxyl group of a fatty acid.
- Hydrophilic
- Attracted to water: charged or polar, so it interacts with water molecules.
- Hydrophobic
- Not attracted to water: non-polar, so it is excluded from water rather than dissolving in it.
Water and inorganic ions
- Polar molecule
- A molecule with an uneven distribution of charge, so that one part is slightly negative and another slightly positive.
- Hydrogen bond
- A weak attraction between a slightly positive hydrogen atom and a slightly negative atom such as oxygen or nitrogen, in another molecule or another part of the same molecule.
- Specific heat capacity
- The energy needed to raise the temperature of one kilogram of a substance by one kelvin.
- Latent heat of vaporisation
- The energy needed to change one kilogram of a liquid into a gas without a change in temperature.
- Inorganic ion
- An ion containing no carbon, apart from carbonate and hydrogencarbonate, present in solution in cytoplasm and body fluids, often in very small amounts, and each with a specific role.
Protein structure and function
- Amino acid
- A molecule containing an amine group, a carboxyl group and a variable side chain attached to the same carbon.
- Polypeptide
- A chain of amino acids joined by peptide bonds.
- Protein
- One or more polypeptides folded into a specific three-dimensional shape.
- Primary structure
- The sequence of amino acids in a polypeptide, held by peptide bonds.
- Secondary structure
- The regular coiling or pleating of the backbone into an α-helix or β-pleated sheet, held by hydrogen bonds between the C=O of one peptide group and the N–H of another.
- Tertiary structure
- The overall three-dimensional fold of a single polypeptide, held by hydrogen bonds, ionic bonds, disulfide bridges and hydrophobic interactions between side chains.
- Quaternary structure
- The arrangement of two or more polypeptides, and any non-protein groups, in a functioning protein.
- Denaturation
- The loss of a protein's specific three-dimensional shape through disruption of the hydrogen bonds, ionic bonds and hydrophobic interactions holding it, so the function is lost, while the primary structure is unchanged.
Also: Cells, microscopy and biological organisation definitions · Enzymes and metabolic control definitions