Properties of Water and Biological Macromolecules

These flashcards cover key concepts related to the properties of water and the formation and functions of biological macromolecules.

Polar Molecule

A molecule with opposite ends carrying opposite partial charges.

Hydrogen Bonds

Attractions between the partial positive hydrogen of one water molecule and the partial negative oxygen of another.

Universal Solvent

Water's ability to dissolve polar molecules and ions, due to its polarity.

Cohesion

Attraction between water molecules, leading to surface tension.

Adhesion

Attraction between water molecules and other polar substances.

Capillary Action

The ability of water to flow in narrow spaces against gravity, due to cohesion and adhesion.

Specific Heat

The amount of heat required to change the temperature of 1 gram of water by 1ºC.

Dehydration Synthesis

The process by which monomers are combined to form polymers, releasing water.

Hydrolysis

The chemical breakdown of a compound due to reaction with water.

Monomer

A single, small unit that can join together to form a polymer.

Polysaccharide

A carbohydrate made up of many monosaccharides linked together.

Glycosidic Linkage

The bond formed between monosaccharides during dehydration synthesis.

Lipids

Hydrophobic organic molecules, generally not forming true polymers.

Saturated Fatty Acid

A fatty acid with no double bonds between carbon atoms, fully saturated with hydrogen.

Unsaturated Fatty Acid

A fatty acid that has at least one double bond, not fully saturated with hydrogen.

Phospholipid

A type of lipid with a hydrophilic head and hydrophobic tails, forming cellular membranes.

Nucleotide

The monomer of nucleic acids, consisting of a sugar, phosphate group, and nitrogenous base.

Peptide Bond

The bond linking amino acids together to form a protein.

Primary Structure

The linear sequence of amino acids in a protein.

Secondary Structure

The folding of the polypeptide chain into alpha helices or beta sheets.

Tertiary Structure

The overall three-dimensional shape of a protein, determined by interactions among R groups.

Quaternary Structure

The structure formed by the interaction of multiple polypeptide chains.