2: Biochemistry of Molecules Flashcards
molecular formula
tells us type and number of atoms
shows molecular weight
polar molecules
carbon hydrogen bonds not soluble so long carbon chains not soluble
polar bonds don’t always equal solubility, its overall balance of molecule
drawing molecules
method 1 = remove showing CH bonds
method 2 = shows only skeleton of carbon chains, no letters implies carbon is bonded to 4 hydrogen
drawing 3D molecules
straight line = normal bond
wedged line = anterior
dashed line = posterior
isomerism
isomers = compounds with same molecular formula but different molecular structures
structural isomers
have same component atoms but arranged differently
chain isomers = chain of carbon atoms is arranged differently
position isomers = location of functional groups is different
function group isomers = different functional groups present
stereoisomers
differ in spatial configuration
geometric isomers = differ in spatial arrangement of atoms or groups on either side of a fixed chemical bond, typical across carbon-carbon double bond, cis or trans formation
optical isomers = compounds with same chemical structure but are non-superimposable mirror images of each other
carbohydrates
carbon hydrogen and oxygen bonded
monosaccharides = 1 molecule of carbohydrate e.g. glucose, fructose, and galactose
condensation reaction occurs (loss of H2O) to form disaccharide
oligosaccharides = 3-10 molecules
polysaccharides = >10 molecules e.g. glycogen
lipids
simplest forms are made up of fatty acids compounds
triglycerides = glycerol with 3 fatty acids bonded
bond via condensation reaction
saturated = single carbon-carbon bonds
unsaturated = double carbon-carbon bonds = harder to break down
amino acids
20 genetically encoded amino acids encoded in our DNA which has 3 letter codes
peptide bond = condensation reaction between carboxyl and amine groups on the end of amino acid chains
dipeptide = two amino acids
polypeptide = more than two
proteins
proteins = long chains of amino acids known as polypeptides
primary structure = determined by the amino acid sequence
secondary structure = formed by alpha helix (left or right hand turn) or beta sheet (parallel or anti-parallel)
tertiary structure = formed by the presence of intermolecular forces
quaternary structure = influenced by the interaction of multiple polypeptide/protein units