Entire Topic 1 Flashcards
- What is a monomer?
- What is a polymer?
- Monomer - smaller units which create larger molecules
- Made from lots of monomers bonded together
What is a condensation reaction?
What is Hydrolisis reaction
Condensation - joining 2 molecules creating a chemical bond and removing water
Hydrolisis - breaking a chemical bond between 2 molecules by using water
What does alpha and beta glucose look like?
What is the bond in disacharides?
- Alpha glucose H ontop of C1 and OH group under
- Beta glucose - OH group ontop on C1 and H group under
Bond: Glycosidic
What is the difference between starch and cellulose and glycogen
Monomers:
Alpha - starch and glycogen
Beta - cellulose
Bonds between monomers:
Starch and glycogen: 1-4 and 1-6 glycosidic bonds
Cellulose: 1-4 glycosidic bonds
Structure
Starch: amylose - unbranched helix, Amylopectin - branched molecule - compact and can fit a lot of glucose in a small space, branched structure increases SA for rapid hydrolisis - insoluble wont affect water potential
Cellulose - forms long straight chain and chains are held in parralel by many hydrogen bonds forming fib rils - this results in productive strength and insolublity
Glycogen - highly branched molecule - increases SA for rapid hydrolisis - wont affect WP
What is the property of triglycerides?
What bonds do fatty acids and glycerol form?
- Energy storage - because of large ratio of carbon hydrogen bonds compared to carbon atoms
- Metabolic water source - High ratio of Hydrogen to oxygen atoms
- Dont affect WP - large and hydrophobic - insoluble in water
- Low mass - can be stored without increasing mass
Ester bond
Property of phospholipids
Hydrophilic head - negative charged phosphate head
Hydrophobic tail - repels H2O
Can therefore form a bilayer - membrane structure
What bond between 2 amino acids?
- Peptide bond?
What is the primary structure?
- Primary - order of amino acids in a polypeptide chain
- Secondary - sequence of amino acids causes parts of protein molecule to bend to alpha helix or beta pleated held by hydrogen bonds
- Tertiary - further folding of secondary structure to form unique 3D shape, held by ionic hydrogen and disulphide bonds
- Quaternary - protein made up of more than 1 polypeptide chain
What are enzymes?
Describe the induced fit model
- tertiary structure proteins which lower activation energy of reactions they catalyse
- Enzymes active site slightly changes shape to fit around substrate and mold
- This movement puts strain on bonds of substrate, therefore weakening bonds
How do each of these effect enzymes:
1. Temp
2. pH
3. Substrate conc.
4. Enzyme conc.
5. Inhibitors
- Temp
- lower: not enough KE for successful collisions between enzyme and substrate
- High: Temp is too high for enzymes to denature, active site changes shape and ES complex cannot form - pH
Both - rapid denaturing of enzyme, will interfere with charges of amino acid, causing ionic and hydrogen bonds to break - Substrate conc.
- fewer collisions between enzyme and substrate - Enzyme conc.
- fewer enzyme active sites
5.
Competitive:
- binds to active site and preents ES complex forming - however more substrate will outcompete inhibitor
Non competitve:
- binds to allosteric site
- causes Active site to change shape
- ES complex cannot form
How do you test starch
- Add iodine
- Positive - turns from orange to blue black
How do you test reducing and non reducing sugars?
Reducing:
1. Add benedics reagents
2. Postiive - turns from blue to green, yellow orange, brick red
Non reducing sugar:
1. After negative reducing test
2. Add acid and boil
3. Cool and neutralise
4. Heat and add benedics reagent
5. Turns orange or brick red
How do you test proteins?
- Add biuret
- Positive would be solution turns from blue to purple
How do you test for lipids?
- Dissolve sample in ethanol
- Add distilled water
- Positive - white emulsion forms
