Topic 1 Biological Molecules Flashcards
3 main functions of lipid
- Insulation
- Energy store
- Protection
Triglycerides
1.Formed condensation of 3 fatty acids and one molecule of glycerol
1.Bonds formed are ester bonds
1.3 bonds formed 3 water molecules formed
How triglycerides structure related to its properties
- High ratio of carbon-hydrogen to c-c good as energy storage molecules
- Fatty acid chain hydrophobic - insoluble doesn’t affect water potential
- Low mass - lots of it can be present in an organism without affecting the ability to walk feed and run which is essential in survival
- Metabolic water source - High ratio of hydrogen to oxygen atoms
Phospholipids
- One fatty acid is replaced by phosphate containing groups
- Condensation reactions between glycerol 2 fatty acid and one phosphate group
How phospholipids structure relates to its properties
- Phosphate group is hydrophilic interacts with water due to the negative charge on oxygen hydrophilic head
- Fatty acid is hydrophobic creates a polar molecule . Forms a phospholipid bilayer
Unsaturated and saturated
Saturated - no double bonds in hydrocarbon chain
Unsaturated - double bonds in hydrocarbon chain
Emulsion test for lipids
- Dissolve sample in ethanol
- Add water and shake
- If lipid present form cloudy white emulsion if negative remains the same
Amino acid
Is a monomer of a protein
Di peptide
1.A condensation reaction between two amino acids forms a dipeptide
2.peptide bond
3. Water molecule removed
Protein structure
- Primary - sequence of amino acids
- Secondary - folding of amino acids into alpha helices or beta - pleated sheats hydrogen bonds hold them together
- Tertiary structure - alpha or beta fold further to form a specific , 3D structure
Ionic and disulphide bridges hold the tertiary structures together hold stability to protein so it can carry out function - Quaternary - more than one polypeptide chain
Polypeptide can bind to a non protein chain.
Biuret test for proteins
- Add biuret reagent
- Shake
- Protein present purple if not remain blue
Enzymes
Proteins
Catalyse reactions by lowering activation energyv
Induced fit model
1.Substare binds to active site
2.substrate induced a conformational change allows substrate bind to active site
3. Forming a substrate enzyme complex
4. Reduces activation energy
How Different conditions affect enzyme activity
Temp-increase temp molecules gain kinetic energy more kinetic energy highly likely that enzyme substrate collide for enzyme substrate complex
Optimum temp - denatures enzyme denatured h bonds broken changing tertiary structure enzyme can no longer bind
Ph- when ph not optimum unbalance of h* and oh- can disrupt tertiary structure alter tertiary substrate not complementary to active site enzyme unactive denatures
Enzyme concentration -steady increase rate of reaction increases rapidly more active site available can bind to substarte
Levels off - not enough substrates some active site left empty rate of reaction no longer increases
Substrate concentartion- more substrate available for active site more enzyme substrate more likely to bind
Levels off - not enough active sites available rate of reaction no longer increases
Enzyme inhibition
Competitive inhibition - competitive inhibitor also complementary to binding site bad as substrate can’t bind
No enzyme substrate can form decreases rate of reaction
Can fix this by increasing the substrate concentration
Non competitive inhibitors -
Tertiary structure of active site changes no longer substrate enzyme complex form
Incrreasw conc can’t fix this