Consolidation 69.69 Flashcards
memorise
Nucleus
- Presence of nuclear envelope: store hereditary material, protect chromatin from rxn in cytoplasm
- Nuclear Pore: regulates exchange of substances between nucleus and cytoplasm
- Nucleolus: site of rRNA synthesis and site of assembly of proteins and rRNA to form ribosomal subunits
Rough endoplasmic reticulum
- To transport of proteins which are synthesised by the ribosomes on its surface to the Golgi apparatus via transport vesicles to be modified and packaged
presence of membrane bound ribosomes
Smooth endoplasmic reticulum
- Synthesis of lipids
- Detoxification of drugs and poisons
Golgi apparatus
Consists of cisternae
* Glycosylate to proteins and lipids to form glycoproteins and glycolipids respectively
* Further modifies, sort and package glycoproteins and glycoplpids into vesicles for secretion out of the cell
* Synthesis of lysosomes
Mitochondrion
circular DNA 70S ribosome
Inner membrane is highly folded to form a cristae: to increase SA to VR to embed more electron carriers to relase more energy for ATP production during oxidative phosphorylation
Chloroplast
circular DNA 70S ribosome
contain chlorophyll which convert solar energy to chemical energy through photosynthesis via light independent reactions and light dependent reactions
contains thylakoid that stack tgt to form intergranal lamella
Centrioles
A pair of hollow cylinders made up of 9 triplets of microtubules
* act as microtubule organising centre (MTOC) during spindle formation in cell division
exp how CSC support the fluid mosiac model?
SIGMA IMPT
- PL molecules arranged in a bilayer
Fluid: - weak HPI b/w PL molecules
- allow PL to move laterally within the bilayer
- kinks in unsaturated fatty acid tails of the PL hinder close packing
- chlestrol b/w the PL hinder close packing
Moasic: - Proteins are embedded in the PL bilayer in a random arrangement
S F of transport protein allow it to carry out its function
- Protein is transmembrane (S) to provide hydrophillic channel for polar molecule to pass across bilayer.
- Exterior of protein has aa residues containing non-polar R groups (S) interact with fatty acid tails of PL molecules via weak HPI
- Contains binding site complementary to ie. glucose for specific transport of the substance
- glucose polar, pass via facilitated diffusion down conc. gradient
Polar molecule repelled by the hydrophobic core of PSB
S F of starch/glycogen
- OH group are face interior of the molecule: Insoluble in water, does not exert osmotic effect on the cell
- Glucose residues joined by alpha−1,4-glycosidic bonds: results in helical coil, more compact for storage. bond can also be hydrolysed by enzymes
- Amylopectin highly branched: provides many sites for enzymes to act on, allows rapid release of glucose
- Anomeric carbon involved in glycosidic bond formation: Stable compound.
MUST LINK TO therefore GOOD STORAGE MOLECULE!!!!
Amylopectin is alpha-1,6-glycosidic bond
S F of Cellulose
- Large Molecule: insoluble in water stored without changing the osmotic potential
- alternate beta glucose molecules inverted, forming linear chians: allows bundling into microfibrils and macrofibrils to increase tensile strength through the crosslink of H2 bonds
- OH grp facing exterior: allow for crosslink of H2 bond b/w adjacent cellulose chains, no OH interact with water, cellulose insoluble
S & F of Haemoglobin
- contains 4 subunits each with haem group contains an iron (II) ion that can bind reversibly with oxygen, allows oxygen binding (in oxygenrich lungs) and release (in metabolically active tissues);;
- four polypeptide chains / subunits allows for cooperative binding as affinity of subunit to oxygen increases after each binding to maximize both oxygen loading and release;;
- hydrophilic amino acid residues present on exterior of each subunit, results in haemoglobin being soluble in red blood cell;;
S & F of Collagen
- every third amino acid of each polypeptide chain is glycine, has H atom as r group, small r group able to fit into centre of triple helix, allows forming of tight compact coil in tropocollagen;;
- extensive hydrogen bonding b/w C=O and N-H group of adjacent amino acid residues to form triple helix –> increase tensile strength
- covalent cross links b/w lysine residues at N and C terminus of of adjacent tropocollagen molecules in staggered arrangement , results in the formation of microfibrils –> increase tensile strength
- microfibrils assembled to form long collagen fibres;;
State the function of DNA and describe how its properties allow it to perform this function.
- DNA stores genetic information;;
- DNA must be chemically stable to encode information without being easily degraded
- DNA must be able to replicate accurately so that the information can be pass down to the next generation
Purpose of cell membrane
- acts as a boundary between interior and exterior of the cell that is selective permeable
- allows for compartmentalisation
- Provides localised environment to facilitate metabolic processes occurring simultaneously
- allows for graident across membranes for the transport of substances
- isolate harmful substances from the rest of the cell
significance of mitosis
Produce genetically identical daughter cells with same number and type of chromosomes for:
* growth by increasing no. of cells
* regeneration and cell repair by replacing damaged cells
* asexual reporduction to produce genetically identical offspring
why need to regulate cell cycle?
- important for growth and development of organism
- prevent uncontrolled cell division and cancer due to dysregulation of cell cycle checkpoints
why is there genetic variation in organism?
- Crossing over between non-sister chromatids of homologous chromosomes in prophase 1 of meiosis: new combinations of alleles
- Independent assortment of homologous chromosomes during metaphase I & random separation of homologous chromosomes during anaphase I: different combinations of paternal chromosomes
- Random fusion of gamete during sexual fertilisation: different genotypes in offspring
how does mutation lead to sickle cell anaemia
take note of the spelling of anaemia!!!
- base pair substitution of the DNA coding for beta globin gene
- Thymine replaced by Adenine
- change in corresponding codon transcribed from GAG to GUG
- Amino acid translated change from hydrophilic glutamic acid to hydrophobic valine
- generates a sticky patch on the surface of the beta-chain subunit
- low oxygen concentrations, sticky patch on haemoglobin is exposed
- adjacent haemoglobin polymerise with each other to form crystalline structures, results in sickle shape
- carries less oxygen, obstruct blood vessel, deprive organ of O2, lead to organ damage
- haemoglobin also haemolyse easily.
fuction of glycoproteins and glycolipids
- acts as cell markers in cell to cell recognition and adhesion for tissue formation
- function as receptors for signal molecules to bind to
effect of non compatitive inhibitor on activity of enzyme
- bind to a site away from the active site of enzyme
- induce a change in the 3d confromation of the enzyme
- active site no longer complimentry to the substrate, subtrate cannot bind to AS and no formation of enzyme substrate complex
- enzyme non functional
competitive inhibitor on activity of enzyme
inhibitor has a 3d conformation complementry to the active site of the enzyme, binds to it, competes with substrate to bind to active site, however can be overcame with high concentration of substrate, maximum rate of reaction reached.
how increase in temp to optimum affect the temp of enzyme
increase temp, increase KE of enzyme and substrate, increase rate of effective collisions b/w substrate and enzyme, increase in rate of formation of enzyme substrate complex, increase in product formation