Biological Molecules Flashcards
Benedict’s test for reducing sugars
Include all monosaccharides + some disaccharides
1. Add Benedict’s reagent to a sample + heat in a water bath that’s been brought to the boil
2. Positive = coloured precipitate (blue to green/yellow/orange/brick red)
Benedict’s test for non-reducing sugars
To test for non-reducing sugars, like sucrose, first you have to break them down into monosaccharides.
- Add dilute hydrochloric acid to a new sample of the test solution, carefully heat in a water bath that’s been brought to the boil
- Neutralise it with sodium hydrogencarbonate
- Carry out the Benedict’s test as you would for a reducing sugar.
- Positive = coloured precipitate
Negative = stay blue, which means it doesn’t contain any sugar (either reducing or non-reducing)
Starch is a mixture of which 2 polysaccharides?
Amylose + amylopectin
Structure of amylose
Long, unbranched chain of alpha-glucose
Angles of the glycosidic bonds give it a coiled structure - makes it compact, so good for storage because you can fit more in to a small space
Structure of amylopectin
Long, branched chain of a-glucose
Side branches allow the enzymes that break down the molecule to get at the glycosidic bonds easily -> glucose can be released quickly
Iodine test for starch
- Add iodine dissolved in potassium iodide solution to test sample
- Positive = colour change from brown/orange to blue/black
Glycogen structure
Structure is similar to amylopectin but has lots more side branches -> stored glucose can be released quickly to release energy in animals
Very compact molecule so good for storage
Cellulose structure
Long, unbranched chains of beta-glucose
When beta-glucose molecules bond, they form straight cellulose chains.
Cellulose chains are linked together by hydrogen bonds to form strong fibres called microfibrils -> provides structural support for plant cell wall
Structure of triglycerides
1 molecule of glycerol + 3 fatty acids
Condensation reaction -> ester bond
Fatty acids structure
Long hydrophobic tails made of hydrocarbons -> insoluble in water
Saturated or unsaturated (in R group)
How does the structure of triglycerides relate to their function?
- Long hydrocarbon tails of fatty acids contain lots of chemical energy so lots of energy released when broken down
- Insoluble so don’t affect water potential of cell + cause water to enter cell by osmosis.
Triglyceride clump together as insoluble droplets in cells with hydrophobic tails facing inwards and hydrophilic glycerol heads facing outwards
Phospholipid structure
1 glycerol molecule + 2 fatty acids + 1 phosphate group
How does the structure of phospholipids relate to their function?
- Heads are hydrophilic + tails are hydrophobic so they form a double layer with heads facing out towards water
- Centre of bilayer is hydrophobic so water-soluble substances cannot easily pass through -> membrane acts as a barrier
Emulsion test for lipids
- Shake test substance with ethanol for a minute so that it dissolves, then pour the solution into water
- Any lipid will show up as a milky emulsion (more lipid = more noticiable milky colour)
Structure of amino acids
Carboxyl group (-COOH), amine group (-NH2) and R group
What bond if formed between amino acids?
Peptide bonds
What is the secondary structure of a protein?
Hydrogen bonds form between amino acids in the polypeptide chain.
Coils into an alpha helix or folds into a beta pleated sheet
What is the quaternary structure of a protein?
The way several different polypeptide chains are held together by bonds
Biuret test for proteins
- Test solution needs to be alkaline so add a few drops of sodium hydroxide solution
- Add copper(II) sulfate solution
Positive = purple
Negative = stay blue
How do enzymes speed up the rate of reaction?
Enzymes lower the activation energy by forming an enzyme-substrate complex
Joining reaction: substrates attached to the enzyme holds them close together, reducing any repulsion between the molecules so they can bond more easily
Breakdown reaction: fitting into the active site puts a strain on bonds in the substrate, so the substrate molecules break up more easily
What is the induced fit model?
- Prior to binding, the substrate and active site and not completely complementary in shape
- When the substrate binds, the active site changes shape and moulds around the substrate
Explains why the enzymes are so specific and only bind to one particular substrate
Why do enzymes denature?
- Higher temperature makes the enzyme’s molecules vibrate more
- If the temperature goes above a certain level, this vibration breaks some of the bonds that hold the enzyme in shape
- Active site changes shape so enzyme + substrate no longer fit together
What is the saturation point in enzyme activity?
All active sites are full so increasing the substrate concentration will have no effect
What is competitive inhibition?
- Competitive inhibitor molecules have a similar shape to substrate molecules so compete with substrate molecules to bind to active site
- Block the active site so no substrate molecules can fit in it
Higher concentration of inhibitor = nearly all active sites full
Higher concentration of substrate = substrate’s chances of getting to an active site before inhibitor increase