Macromolecules and Proteins Flashcards
what are the 4 major families of small organic molecules and the subunits and macromolecules
sugars -> polysaccharides
fatty acids -> fats/lipids/membranes
amino acids -> proteins
nucleotides -> nucleic acids
what reaction forms macromolecules
condensation = covalent bond through loss of water
hydrolysis (reverse) = break apart with water
require ATP and catalyst
what is the simplest sugar
monosaccharides
- have 6 carbon ring
types of sugars and uses
starch = storage
cellulose = building material
What is the one group that does not form polymers
Lipids
Grouped because they are insoluble in water (soluble in fats/oil)
Structure of fatty acids
Long hydrocarbon chain (hydrophobic)
Carboxyl group (-COOH) (hydrophilic)
Structure of glycerol
Alcohol
3 Carbons each with hydroxyl group (-OH)
Structure of Phospholipids
Glycerol with
- 2 fatty acids (hydrophobic tail)
- 3rd hydroxyl group joined to phosphate group (hydrophilic head)
How do glycerol and fatty acids bond
Form covalent bond though dehydration reaction with hydroxyl group
Types of proteins
- enzyme - catalyse reactions
- gene regulation - switch on/off
- structure
- transport - though membranes, around body (haemoglobin)
How do membranes form
Double layer of phospholipids arrange themselves with the hydrophobic tails on the interior and the hydrophilic heads on the outside to aqueous environments to minimise free energy
= phospholipid bilayer
Structure of Amino Acid
C
H
- Carboxyl group (-COOH)
- Amino group (NH2)
- R group
What type of bond forms between AA in creating proteins
Peptide bonds
Link C1 to N2
What is the primary protein structure
Specific sequence of AA that make up the protein chain
What is the secondary protein structure
Hydrogen bonds between H and O in amino and carboxyl groups twist chains into coils or sheets
What is the protein tertiary structure
R groups interact by
- ionic bonds
- disulphide bridge
- H bonds
- hydro interactions
to create 3D shape depends on AAs
What is protein quaternary structure
Multiple polypeptide chains associate to form a functional protein
How can mutations / substitutions in amino acids impact protein function
- if mutation in codon, most likely will still encode for same AA anyway due to redundancy
- If different AA may result in very different overall shape and therefore function
- Sickle cell example
