1. Biological Molecules
1.1. polysaccharides
1.1.1. starch
1.1.1.1. amylase
1.1.1.2. amylopectin
1.1.2. glycogen (in animals)
1.1.3. cellulose
1.1.3.1. made up of B-glucose
1.1.4. glycosidic bond
1.2. monosacharrides
1.2.1. thousands of monosacharrides forming polysaccharides
1.2.2. 3 carbon atoms
1.2.2.1. triose
1.2.3. 5 carbon atoms
1.2.3.1. pentose
1.2.4. 6 carbon atoms
1.2.4.1. hexose
1.3. recognized by antibodies and lymphocytes
1.4. disacharrides
1.4.1. formed when 2 monosacharrides linked together
1.4.2. glycosidic bond
1.5. lipids
1.5.1. alcohol
1.5.1.1. cobtains hydroxyl group (-OH) attached on carbon atom
1.5.2. fatty acid
1.5.2.1. cobtains carboxyl group (-COOH)
1.5.2.1.1. saturated
1.5.2.1.2. unsaturated
1.5.3. all are insoluble in H2O
1.5.3.1. fats
1.5.3.2. oil
1.5.4. lipids are ester
1.5.4.1. fatty acid + alcohol
1.6. protein
1.6.1. peptide bond formed by condensation between 2 amino acids, forming dipeptide
1.6.2. protein structures
1.6.2.1. primary structure
1.6.2.1.1. sequence of amino acids that makes up polypeptide chains
1.6.2.2. secondary structure
1.6.2.2.1. polypeptide chains may be twisted
1.6.2.3. tertiary structure
1.6.2.3.1. the compact structure of a protein molecules resulting from the 3D coiling of the already folded chain of amino acid
1.6.2.4. quaternary structure
1.6.2.4.1. 3D arrangement of two or more polypeptide
1.6.2.4.2. or polypeptide and non-protein component
1.7. phospholipids
1.7.1. contains fatty acid tails
1.7.2. has hydrophilic head containing phosphate group
1.8. triglyceride
1.8.1. insoluble in H2O
1.8.2. non-polar nature of hydro carbon tails
1.9. glycerol
1.9.1. an alcohol group with 3 hydroxyl group
2. Cell Membrane and Transport
2.1. Diffusion
2.1.1. movement of ions from high to low concentration
2.2. Osmosis
2.2.1. movement of water molecules from high to low concentration
2.3. Endocytosis
2.3.1. engulfing a particle from outside the cell
2.4. Exocytosis
2.4.1. releasing their contents to the outside cell
2.5. components of phospholipids bilayer
2.5.1. Clycoprotein & Glycolipid
2.5.1.1. receptors
2.5.1.2. promotes adnesion
2.5.2. transport protein
2.5.2.1. carrier
2.5.2.1.1. provide pathways
2.5.2.1.2. diffusion, osmosis and active transport
2.5.2.2. channel
2.5.2.2.1. also provide pathways
2.5.2.2.2. active transport only
2.5.3. phospholipids
2.5.3.1. glycerol
2.5.3.2. 2 fatty acid
2.5.3.3. a phosphate group
2.5.4. cholesterol
2.5.4.1. regulate the activity of intergral protein
2.6. cell signaling
2.6.1. glycoproteins
2.6.1.1. release of the signaling molecules by signaling cell
2.6.1.2. transport of the signal to target cell
2.6.1.3. binding of the signal to its specific receptor for activation
2.6.1.4. opening of signal - transduction pathways
3. Cell Structure
3.1. animal cells
3.1.1. centrioles
3.1.1.1. involved in the assembly of microtubules to form fibre
3.2. both
3.2.1. nucleus envelope
3.2.1.1. separate nucleus from cytoplasm
3.2.1.2. allow movement of substance
3.2.2. nucleus
3.2.2.1. store of energetic info
3.2.3. necleous
3.2.3.1. produce ribosomes
3.2.4. mitochondria
3.2.4.1. ATP production for aerobic respiraton
3.2.5. microtubule
3.2.5.1. provide pathways
3.2.5.2. form fibres and cytoskeleton
3.2.6. lysosome
3.2.6.1. surrounded by enzymes
3.2.6.2. to destroy worn out parts
3.2.6.3. to digest foreign substances
3.2.7. golgi body
3.2.7.1. modify protein
3.2.7.2. make vesicles to make lysosome
3.2.8. ribosomes
3.2.8.1. manufacture amino acid to male polypeptide
3.2.9. smooth ER
3.2.9.1. make triglycerides, phospholipids and cholesterol
3.2.10. cell membrane
3.2.10.1. control exchange of substance
3.2.10.2. retains cell contains
3.2.10.3. cell boundary
3.2.11. rough ER
3.2.11.1. modify protein
3.2.11.2. transport them to golgi body
3.3. plant cells
3.3.1. cell wall
3.3.1.1. provide support
3.3.2. large vacuole
3.3.2.1. storing substances
3.3.2.2. creating pressure to provide support
3.3.3. plasmodesma
3.3.3.1. allow substance to move without crossing cell surface membrane
3.3.4. chloroplast
3.3.4.1. photosynthesis occurs
4. Enzymes
4.1. globular protein
4.1.1. catalyze metabolic reactions
4.1.2. lowering activation energy
4.2. has active sites
4.2.1. change shape slightly to fit substance
4.2.2. called induced fit hypothesis
4.2.3. when substrate enters, enzyme-substrate complex formed
4.3. factors affecting activity
4.3.1. substrates concentration
4.3.1.1. higher concentration = faster rate of reaction
4.3.1.1.1. if enough enzyme
4.3.2. enzyme concentration
4.3.2.1. higher concentration = faster rate of reaction
4.3.2.1.1. if enough substrate
4.3.3. Temperature
4.3.3.1. higher temperature = faster rate of reaction
4.3.3.2. works best at optimum temperature
4.3.3.3. denatures above optimum temperature
4.3.4. pH
4.4. immobilized enzyme
4.4.1. advantage
4.4.1.1. purification is not needed
4.4.1.2. enzyme recover more rapidly
4.4.1.3. enzymes are more stable
4.5. inhibitor
4.5.1. competitive
4.5.1.1. has similar shape to normal substrate
4.5.1.2. compete with substrate for active site
4.5.1.3. is reversible
4.5.1.3.1. inhican enter and leave active site
4.5.2. non-competitive
4.5.2.1. bind permanently to active site
4.5.2.2. bind a site on the enzyme
4.5.2.2.1. change in shape of active site
4.5.2.3. may or may not be reversible