Test for non-reducing sugars
Boil with acid AND neutralise
Heat with benedicts
Red precipitate
Difference between cellulose and glycogen
Cellulose made of Beta glucose
Glycogen made of alpha glucose
Cellulose has straight chain
Glycogen is branched
Cellulose has straight chain
Glycogen is coiled
Cellulose has 1-4 glycosidic bonds
Glycogen has 1-4 AND 1-6 glycosidic bonds
Features of starch which make it a good storage molecule
Insoluble - Doesnt affect water potential
Branched/Helical - Makes molecule compact
Large molecule - Cannot cross cell membrane
More ends - Fast enzyme action
Structure of glycogen
Polymer of alpha glucose
Joined by glycosidic bonds
How does glycogen act as a source of energy
Hydrolysed to glucose
Glucose used in respiration
How is cellulose adapted to its function
Long and straight chains
Become linked together by many hydrogen bonds to form fibrils
Provide strength to cell wall
How to test for presence of a lipid in a sample of food
Add ethanol
THEN add water
AND shake
Milky/White emulsion
How is triglyceride molecule formed
ONE glycerol and THREE fatty acids
Condensation reactions AND removal of THREE molecules of water
Ester bonds formed
How is ester bond formed in phospholipid
Condensation reaction
Between glycerol and fatty acid
Describe the induced fit model
Substrate binds to the active site
Active site changes shape slightly so it is complementary to substrate
How do competitive inhibitors decrease the rate of enzyme controlled reactions
Inhibitor similar shape to substrate
Binds to active site
Reduces enzyme substrate complexes forming
How does the structure of a protein vary depending on the amino acids it contains
(5 Marks)
Structure is determined by position of amino acid
Primary structure is sequence of amino acids
Secondary structure formed by hydrogen bonding
Tertiary structure formed by interactions
Creates active sites in enzymes
Quarternary structure contains multiple polypeptide chains
How does active site of enzyme cause a high rate of reaction
Lowers activation energy
Induced fit causes active site to change shape
Enzyme substrate complex causes bonds to break
Describe the test for a protein in a solution
Add biuret reagent
Positive result - Purple/Lilac
Similarities between dipeptides
Amine group (NH2) at end
Carboxyl group (COOH) at end
2 R groups
All contain C and H and N and O
Difference between dipeptides
Different R groups
How do non competitive inhibitors reduce the rate of an enzyme controlled reaction
Attaches to the enzyme at a site other than the active site
Changes shape of active site
So active site and substrate are no longer complementary
So no substrate can bind
Describe how a peptide bond is formed between two amino acids to form a dipeptide
Condensation reaction
Between amine group and carboxylic group
How is the secondary structure of a polypeptide produced by binds between amino acids
Hydrogen bonds
Forming beta pleated sheets
Or
Forming alpha helix
Why can 2 proteins have the same number and type of amino acids but different tertiary structures
Different sequence of amino acids
Forms ionic/hydrogen/disulfide bonds in different places
How does a formation of an enzyme substrate complex increase the rate of reaction
Reduces activation energy
Due to bending bonds
What is the definition of a genetic code
More than one codon codes for a single amino acid
Variables that can be controlled in an enzyme controlled reaction
Initial substrate concentration
Enzyme concentration
pH
Describe the structure of DNA
Polymer of nucleotides
Each nucleotide formed from deoxyribose, a phosphate group and organic base
Phosphodiester bonds between nucleotides
Double helix held by hydrogen bonds
Pairing between adenine, thymine, guanine and cytosine