Biological Molecule Flashcards
Structural characteristics of starch
- compact
- helical
- insoluble, doesn’t affect water potential
- large, cannot leave cell
- 1-4 1-6 glycosidic bond
Structural characteristics of cellulose
- long straight chains
- 1-4 glycosidic bond
- beta glucose
- flip 180
- form microfibrils
- H bonds hold chains together= strength
Structural characteristics of glycogen
- 1-4 1-6 glycosidic bond
- made up of alpha glucose
- highly branched ( more than starch) and coiled chains
methods used to measure quantity of reducing sugar
- use colorimeter and calibration curve
- (without using colorimeter) filter and dry precipitate, find mass or weight comparison
5 roles of lipids
- make up cell membrane, e.g. phospholipid contribute to flexibility of membrane and transfer of lipid soluble substance across them
- soucrce of energy
- waterproofing
- insulation
- protection
Lipids role of waterproofing
insoluble, plants and insects have waxy lipid cuticle that conserves water. Mammals produce oil secretion from the sebaceous glands in skin
Lipids role as source of energy
- when oxidised, lipids provide more than twice the energy as carbohydrates and release valuable water
Lipids role of insulation
- fats are slow conductors of heat help retain body heat.
Lipids role of protection
- often store around delicate organs like kidney
Structure of lipids
- made of CHO, greater ratio of H:O of 2:1and long hydrocarbon chains (R group)
- not polymers because no repeating units, not a continuous chain
Saturated fatty acid
- only with single C-C bond
- typically more reactive
- solid at room temperature
- typically unhealthy fats
Unsaturated fatty acid
- with one or more double C=C bond
- one double bond is mono unsatured
- two or more double bond is polyunsaturated
- liquid in room temp, typically healthier oils
Triglycerides structure to functions
- low mass to energy ratio so a good storage molecules because a lot of energy can store in a small volume
- it is large, non polar molecules, insoluble so doesn’t affect osmotic balance or water potential
- high ratio of H to O atoms, it release water when oxidised, provide a source of water
Phospholipids structure
- 1/3 fatty acid replaced by a phosphate molecule
- it has a hydrophilic head and hydrophobic tail
- It is a polar molecule
Phospholipids structure to properties
- in aqueous environment, it form a bilayer within cell surface membranes. So a hydrophobic barrier is formed between inside and outside of a cell
- hydrophilic head help to hold the surface of cell surface membranes
- allow to form glycolipids by combining carbohydrate within cell surface membranes. Glycolipids are important in cell recognition
Test for lipids
- add 5cm3 ethanol in a 2cm3 sample, shake gently to let them dissolve. And water and shake again.
- a cloudy white emulsion indicates the presence of lipids
Why is ethanol test results in cloudy white? 🤍
Because lipids is being finely dispersed in the water to form emulsion. Light will be refracted when passing through from oil droplets to water droplets, making it appear cloudy
Four groups attached with a central carbon atom
- amino group NH2
- hydrogen atom
- carboxyl group COOH
- R group( variety of different chemical groups, each amino acid has different R group)
How is dipeptide formed?
- condensation reaction of two amino acids with the form of peptide bonds
- the water is made of OH in the carboxyl group of one and H in the amino group of the other
Primary structure of a polypeptide
- the sequence of amino acids of a polypeptide chain forms the primary structure of a protein
- the sequence is determined by DNA, and it determines the ultimate shape and function of the protein
- change in shapes will change the function of the protein
Secondary structure of protein
- the H in NH is positive and O of the C=O is negative so they readily form a weak hydrogen bonds , caused the long peptide bond to twist into 3D coil, α- helix shape or β pleated sheet
- hydrogen bonds are easy to break
Tertiary structure of protein
- α- helix structure can be twisted and fold even more to give complex 3D shape
- it is maintained by disulfide bridges, ionic bonds and more hydrogen bonds
- this allows protein to be distinctive and can be recognised by other molecules
Properties of different bonds form in protein
Disulfide bridges- very strong, not sure easy to break
Ionic bonds- formed between carboxyl and amino group, not involved in forming peptide bonds. Weaker than disulfide bridges, can easily break by change in PH
Hydrogen bonds- easily broken
Quaternary structure of proteins
- few polypeptide chains link together
- sometimes non protein components are added e.g. iron of haem group to make haemoglobin