Outline the control of metabolism by end-product inhibition.
a. end-product of a metabolic pathway inhibits an enzyme earlier in the pathway
b. end-product binds to allosteric site of enzyme
c. changes shape of active site of enzyme
d. enzyme activity reduced/stopped when end-product binds
e. production of end-product reduced/stopped when enzyme inhibited
f. production resumes when end-product used up/concentration of end-product falls
g. example of end-product inhibition
Outline the functions of rough endoplasmic reticulum and Golgi apparatus.
Rough Endoplasmic Reticulum (RER)
- Synthesis of proteins/polypeptides
1 mark - Ribosomes on surface/attached to RER
1 mark - Proteins for secretion/export/use outside cell OR proteins for use in lysosomes/cell membrane
1 mark - Modification/processing/folding of proteins
1 mark - Synthesis/processing of lipids/phospholipids
1 mark - Storage of calcium ions
1 mark
Golgi Apparatus
- Further modification/processing of proteins
1 mark - Packaging/vesicle formation of proteins for secretion/export
1 mark - Formation of lysosomes
1 mark - Synthesis/processing of carbohydrates/glycoproteins/glycolipids
1 mark
Explain how hydrophobic and hydrophilic properties contribute to the arrangement of molecules in a membrane.
a. Hydrophilic is attracted to/soluble in water and hydrophobic not attracted/insoluble
b. Hydrophilic phosphate/head and hydrophobic hydrocarbon/tail in phospholipids
c. Phospholipid bilayer in water/in membranes
d. Hydrophilic heads of phospholipids face outwards/are on surface
e. Hydrophobic tails of phospholipids face inwards/are inside/are in core
f. Cholesterol is mainly hydrophobic/amphipathic so is located among phospholipids/in hydrophobic region of membrane
g. Some amino acids are hydrophilic and some are hydrophobic
h. Hydrophobic amino acids/regions of proteins in phospholipid bilayer core
i. Hydrophilic amino acids/regions of proteins are on the membrane surface
j. Integral proteins are embedded in membranes due to hydrophobic properties/region OR transmembrane proteins have a hydrophobic middle region and hydrophilic ends
k. Peripheral proteins on are on the membrane surface/among phosphate heads due to being entirely hydrophilic OR carbohydrate part of glycoproteins is hydrophilic so is outside the membrane
l. Pore of channel proteins is hydrophilic