topic 1 Flashcards
What is a monomer?
a smaller / repeating) unit / molecule from which larger molecules / polymers are made;
What is a polymer?
made up of many identical / similar molecules / monomers / subunits
Condensation reaction
joins two molecules together with the formation of a chemical bond and involves the elimination of a molecule of water
Hydrolysis reaction
breaks a chemical bond between two molecules and involves the use of a water molecule
Bonds in:
Lipids
Proteins
Carbohydrates
DNA
Ester = lipids
Peptide = proteins
Glycosidic = carbohydrates
Phosphodiester = DNA
Monosaccharides in
disaccharides:
Lactose
Sucrose
Maltose
Glucose and galactose = lactose
Glucose and fructose = sucrose
2 glucose = maltose
Alpha and beta
glucose structure
Structure: C6H12O6
Alpha: OH group below
Beta: OH group above
Comparing cellulose
and glycogen
- Cellulose is made up of β-glucose (monomers) and glycogen is
made up of α-glucose (monomers); - Cellulose molecule has straight chain and glycogen is branched;
- Cellulose molecule has straight chain and glycogen is coiled;
- glycogen has 1,4- and 1,6- glycosidic bonds and cellulose has only 1,4- glycosidic bonds;
Starch structure and
function
- Insoluble (in water), so doesn’t affect water potential;
- Branched / coiled / (α-)helix, so makes molecule compact;
OR
Branched / coiled / (α-)helix so can fit many (molecules) in small area; - Polymer of (α-)glucose so provides glucose for respiration;
- Branched / more ends for fast breakdown / enzyme action;
- Large (molecule), so can’t cross the cell membrane
Cellulose structure
and function
- Long and straight chains;
- Become linked together by many hydrogen bonds to form fibrils;
- Provide strength (to cell wall).
Describe how an
ester bond is formed in a phospholipid
molecule.
- Condensation (reaction) OR Loss of water;
- Between of glycerol and fatty acid;
Unsaturated fatty
acids
Double bonds (present) / some / two carbons with only one hydrogen / (double bonds) between carbon atoms / not saturated with hydrogen;
Triglycerides
compared to
phospholipids
- Both contain ester bonds (between glycerol and fatty acid);
- Both contain glycerol;
- Fatty acids on both may be saturated or unsaturated;
- Both are insoluble in water;
- Both contain C, H and O but phospholipids also contain P;
- Triglyceride has three fatty acids and phospholipid has two fatty
acids plus phosphate group; - Triglycerides are hydrophobic/non-polar and phospholipids have
hydrophilic and hydrophobic region;
Accept ‘non-polar’ for hydrophobic and ‘polar’ for hydrophilic. - Phospholipids form monolayer (on surface)/micelle/bilayer (in
water) but triglycerides don’t;
Amino acid structure
H, NH2, COOH bonded to a central carbon and then a variable R group
Protein structure
- Structure is determined by (relative) position of amino acid/R
group/interactions; - Primary structure is sequence/order of amino acids;
- Secondary structure formed by hydrogen bonding (between amino
acids); - Tertiary structure formed by interactions (between R groups);
- Creates active site in enzymes OR Creates complementary/specific
shapes in antibodies/carrier proteins/receptor (molecules); - Quaternary structure contains >1 polypeptide chain OR Quaternary
structure formed by interactions/bonds between polypeptides
Enzyme action
- Reduces activation energy;
Accept ‘reduces E a ‘. - Due to bending bonds
OR
Without enzyme, very few substrates have sufficient energy for reaction
Enzymes and
temperature
- At low temperatures, molecules have less kinetic energy
- So less successful collision/less enzyme-substrate complexes form
- At higher temperatures (above optimum) denaturation is due to more
(kinetic) energy; - Breaks hydrogen / ionic bonds (between amino acids / R groups);
- Change in shape of the active site / active site no longer
complementary so fewer enzyme-substrate complexes formed / substrate does not fit;
Induced fit model
- Substrate is not complimentary to the enzyme active site.
- Active site alters shape to fit around substrate/forms an enzyme-
substrate complex - Bonds are stressed/bent
Competitive inhibitor
action
- Similar shape to the substrate/complimentary to the enzyme active
site - Binds to active site
- So less enzyme-substrate complexes can form
Non-competitive
inhibitor action
- Attaches to the enzyme at a site other than the active site;
Accept ‘attaches to allosteric/inhibitor site’ - Changes (shape of) the active site
OR
Changes tertiary structure (of enzyme); - (So active site and substrate) no longer complementary so less/no
substrate can fit/bind
DNA nucleotide
Deoxyribose Sugar, Bases GCAT, and Phosphate Group
DNA replication
- Strands separate / H-bonds break;
- DNA helicase (involved);
- Both strands / each strand act(s) as (a) template(s);
- (Free) nucleotides attach;
- Complementary / specific base pairing / AT and GC;
- H-bonds reform;
- DNA polymerase joins nucleotides (on new strand);
- Reject: if wrong function of DNA polymerase
- Forming phosphodiester bonds
- Semi-conservative replication / new DNA molecules contain one old strand and one new strand;
- Reject: if wrong context e.g. new DNA molecules contain half of each original strand
DNA polymerase
function
- Joins (adjacent DNA) nucleotides;
- (Catalyses) condensation (reactions);
- (Catalyses formation of) phosphodiester bonds (between adjacent nucleotides)
DNA structure to
function
- Weak / easily broken hydrogen bonds between bases allow two strands to separate / unzip;
- Two strands, so both can act as templates;
- Complementary base pairing allows accurate replication