Monomers are linked together to form polymer chains, with a water molecule formed in the process
What is a hydrolysis reaction?
The breaking down of polymers into monomers by the addition of water molecules
What are the 3 main monosaccharide?
Glucose
Galactose
Fructose
What is glucose?
A hexose sugar (6 carbons) that can form two isomers (α-glucose and β-glucose)
Alpha glucose molecules can bond together to form starch or glycogen
Beta glucose molecules can bond together to form cellulose
What is starch?
A mixture of two polysaccharides, amylose and amylopectin, used by plants to store excess sugar
What is amylose
Made from α-glucose 1,4 – glycosidic bonds, compact coiling for efficient storage
Insoluble, doesn't affect water potential
Amylopectin
Made from α-glucose 1,6 and 1,4 – glycosidic bonds, branched structure increases surface area for rapid hydrolysis
Insoluble, doesn't affect water potential
Cellulose
Made up of Beta glucose, forms long unbranched chains that can cross-link via hydrogen bonds to provide structural support in plant cell walls
Cellulose
Provides rigid cell walls to prevent plant cells from bursting due to osmosis, maintaining turgidity for photosynthesis
Glycogen
Made up of α-glucose, a highly branched polysaccharide used by animals to store excessglucose
Glycogen
Many branches to increase surface area for rapid hydrolysis, very compact for efficient storage, insoluble
Lipids
Insoluble in water but soluble in organic solvents, main groups are triglycerides and phospholipids
Roles of lipids
Source of energy
Waterproofing
Insulation
Triglycerides
Consist of 1 glycerol molecule joined to 3 fatty acid chains via ester bonds, non-polar
Fatty acids
Long chain organic compounds that can be saturated, unsaturated, or polyunsaturated
Phospholipids
Consist of a glycerol molecule, a phosphate, and 2 fatty acid chains, polar head and non-polar tails allow them to form bilayers in cell membranes
Proteins
Large molecules made up of amino acids, with 20 different amino acids present in all life forms
Levels of protein structure
Primary
Secondary
Tertiary
Quaternary
Enzymes
Biological catalysts that lower the activation energy of reactions, have a specific active site complementary to the substrate
Induced fit model
The active site of an enzyme changes shape slightly to mould around the substrate, putting strain on the substrate bonds and lowering activation energy
Factors affecting enzyme activity
pH
Temperature
Concentration
Competitive inhibition
Inhibitors that bind directly to the active site of an enzyme, competing with the substrate
The concentration of competitive inhibitors compared to the concentration of substrates determines the effect of enzyme activity
If substrate concentration is increased, the effect of the competitve inhibitor is reduced as the inhibitor is not permanently bound to the active site
Inhibitors
Substances that directly or indirectly interfere with the function of the active site of an enzyme which leads to reducing its activity
Types of inhibitors
Competitive inhibitors
Non-competitive inhibitors
Competitive inhibitors
Bind directly to the active site of the enzyme
Have a molecule shape similar to that of the substrate, allowing them to bind directly to the active site
Compete with the substrate for the available active sites
Non-competitive inhibitors
Attach themselves to an alternate binding site called the allosteric site
Alter the shape of the enzyme and therefore the shape of its active site
Substrate molecules are unable to fit into the enzyme, so it is unable to function
Increase in substrate concentration does not alter the enzyme activity because the substrate and the inhibitor are not competing
Reducing Sugars Test
1. Add excess Benedict's reagent to the sample and heat in a warm water bath and wait for a colour change
2. If the reducing sugar is present a green/yellow/red precipitate is formed, if not the solution remains blue
Non-Reducing Sugars Test
1. Add dilute Hydrochloric acid and heat in a water bath (to break bonds and produce monosaccharides)
2. Add an alkali to neutralise (NaOH)
3. Conduct the test for reducing sugars
Starch Test
Add iodine to the sample, there will be a colour change from brown/orange to blue/black
Proteins (presence of amino acids) Test
1. Add excess biuret reagent to the sample, shake and leave at room temperature
2. If there are amino acids present then a purple/lilac precipitate forms, if not the solution will remain blue
Lipids (emulsion) Test
1. Add ethanol to the sample then add water, shake for a minute
2. If lipids are present, they will form a milky white emulsion (layer above the ethanol/water)
Nucleotide
Made up of a pentose sugar, a phosphate group and a nitrogenous base
Ribonucleic Acids (RNA)
Single polynucleotide chain with ribose as the pentose sugar and the organic bases can be adenine, uracil, guanine and cytosine
Deoxyribonucleic Acids (DNA)
Double helix shape with deoxyribose as the pentose sugar and the nitrogenous bases are: adenine, thymine, guanine and cytosine
Made up of two nucleotide strands with hydrogen bonds between complimentary base pairs
DNA Replication
1. DNA helicase causes the two strands to unwind
2. Free nucleotidesbind to their complimentary bases on the template strands
3. DNApolymerase creates phosphodiester bonds between the adjacent nucleotides on the phosphate backbone.
4. Results in two identical strands of DNA, each containing half of the original strand (semi-conservative model)
ATP
Phosphorylated macromolecule with three parts: adenine, ribose and a chain of 3 phosphates
Bonds between the phosphate groups are unstable and have a low activation energy, when these bonds are broken, they release a considerable amount of energy
ATP Synthesis
Addition of a phosphate molecule to ADP, can occur during photosynthesis, respiration, or phosphate group transfer
Roles of ATP
Not a good long-term energy store due to the instability of the bonds between phosphate
Provides energy for metabolic processes, movement, active transport, secretion, and activation of molecules