Unit B 死记烂背 Flashcards
B1,1
3 Properties of carbon allowing chemical diversity
- Carbon forms covalent bonds
- Carbon forms up to 4 single bonds, or combination of bonds
- Forms straight/branched chains or single/multiple rings
B1.1
4 Properties of monosaccharides
- Solubility
- Transportability
- Chemical stability
- Oxidation yields energy
B1.1
4 Properties of glucose
- Solubility – dissolves in water as it is polar
- Transportability – dissolves in blood plasma
- Chemical stability – cyclic molecule with -OH in axial region
- Oxidation yields energy – respiration releases energy
B1.1
4 Forms of storage of glucose
- Amylose (eg. potatoes) – linear starch chain linked by a-1,4-glycosidic bonds
- Amylopectin (main component) (eg. corn) – starch chain linked by a-1,4-glycosidic bonds, with branches joined by a-1,6-glycosidic bonds every 24-30 units
- Cellulose – linear chain linked by b-1,4-glycosidic bonds, cross-linked by H-bonds and bundled into microfibrils
- Glycogen – chain linked by a-1,4-glycosidic bonds, with branches joined by a-1,6-glycosidic bonds every 8-12 units
B1.1
4 Functions of glycoproteins
- Cell-cell recognition
- Receptors
- Ligands
- Structural support
eg. ABO blood antigens
B1.1
3 differences in properties of saturated/unsaturated lipids
- Solid/liquid at RTP
- High/low viscosity
- High/low melting point
B1.1
Storage of fats in plants and endotherms
- Plants – unsaturated fats and oils in seeds for germination
- Endotherms – liquid droplets in adipocytes for respiration
B1.2
7 Functions of proteins with examples
- structure (macro/micro) –- collagen/histone
- transport (extra/inter/intracellular) –- haemoglobin/ channel protein
- enzyme –- lysozyme
- movement –- actin / tubulin
- hormones –- insulin
- antibodies –- immunoglobulin
- storage –- albumin
B1.2
4 examples of types of R-group
- Acidic – aspartic acid
- Basic – lysine
- Polar – serine
- Non-polar – alanine
B1.2
Origins of H-bonds, S-bonds and ionic bodns in proteins
- H-bonds – between polar hydrophilic R-groups
- S-bonds – between cysteine residues
- ionic bonds – between NH2 or C=O charged by binding/dissociation of H+, and charged R-groups
B1.2
Levels of Polypeptide Structure
Primary Structure - sequence of amino acids, linked by peptide bonds
Secondary Structure – local folding of peptides into a-helices or b-pleated sheets
Tertiary Structure - folding of polypeptide via H-/S-/ionic bonds
Quaternary Structure - arrangement and interaction of two or more polypeptide chains to form a functional protein
B1.2
Conjugation in Haemoglobin, Insulin and Collagen
- Haemoglobin – tetramer with haem groups and iron
- Insulin – non-conjugated dimer
- Collagen – non-conjugated trimer
B1.2
4 Properties of Globular Proteins
- Tertiary structure, often spherical in shape
- Water-soluble
- High pH/temperature sensitivity
- Function as enzymes, transporters, regulators
eg. Insulin has a hydrophilic exterior to be transported in blood plasma, but a hydrophobic core to be chemically stable
B1.2
4 Properties of Fibrous Proteins
- Secondary structure, often linear or long in shape
- Water-insoluble
- Low pH/temperature senstivity
- Function as structural support and stabilisation
eg. Collagen is made of 3 twisted H-bonded polypeptides containing glycine, proline, and hydroxyproline
B2.1
7 Point Explanation of Cholesterol Effect on Membrane Fluidity
- Polar group faces aqueous external environment
- Non-polar regions face interior of bilayer
- Rigid steroid structure strongly interacts with phospholipids
- Increases fluidity at low temperature by interfering with packing of fatty acid chain
- Decreases fluidity at high temperature by reducing mobility of phospholipis
- Broadens phase transition of freezing
- Prevents abrupt membrane fluidity changes
B2.1
7 Point Explanation of Effect of Temperature on Fatty Acid Saturation
- Unsaturated tails are kinked so are less dense and have lower melting point
- At low temperature, less saturation to prevent membrane solidification
- Membrane fluidity needed for protein function
- Saturated tails are straight, so can be more tightly packed leading to higher melting point
- At high temperature, more saturation to strengthen membrane
- To maintain appropriate membrane fluidity
- Eg. cold-blooded organisms and hibernating animals
B2.1
Example of ligand-gated channel in a neuron (3)
Nicotinic acetylcholine receptors
- Postsynaptic receptors have acetylcholine/nicotine binding site
- Binding causes a reversible conformational change allowing inward facilitated diffusion of 5 sodium ions
- Influx of sodium depolarises membrane, helping to generate the action potential
B2.1
Example of voltage-gated channel in a neuron (3)
Sodium/Potassium channels
- Ball-and-chain mechanism controls opening of the membrane
- Voltage change causes a conformational change in the pore, causing the ball to detach allowing sodium influx/potassium efflux
- Influx of sodium depolarises membrane, potassium efflux repolarises membrane
B2.1
Example of direct active transport (5)
Sodium-Potassium Pump
- Pump is open to inside of cell. Sodium ions bind to 3 binding sites
- Binding triggers ATP hydrolysis. Pi binds to pump, causing a conformational change.
- Pump is open to outside of cell. Potassium ions bind to 2 binding sites.
- Bindings triggers release of Pi from pump, causing a conformational change.
- Bidirectional active transport builds a high Na+ concentration outside and high K+ concentration inside the cell to reestablish membrane potential after hyperpolarisation.
B2.1
4 Point Explanation of Role of Phospholipids in Plasma Membrane
- hydrophilic phosphate faces aqueous external environment
- hydrophobic fatty acids face each other forming core
- low permeability to large or charged species
- effective patrtial permeability
B2.1
5 Functions of Proteins in Membranes
- Facilitated diffusion and Active transport
- Cell recognition
- Cell adhesion
- Chemical reception
- Enzymes
B2.1
3 Functions of glycocalyx
- Cell recognition
- Cell adhesion
- Cell signalling
B2.1
Role of aquaporins in transport of water (3)
- Aquaporins are tetramers of water channels with hydrophilic R-groups
- Hydrophilic R-groups attract polar H2O by hydrogen bonds
- H2O molecules bidrectionally pass through each channel in single file
B2.1
5 Point Explanation of Function of Endocytosis and Exocytosis
- Endocytosis - formation of vesicles by inward pinching of membrane
- Exocytosis - fusion of vesicles with membrane
- Possible due to strength and fluidity of fluid mosaic membrane
- Energy needed in form of ATP to transport vesicles
- Eg. phagocytosis; and synaptic transmission