“alular Functions aa 2018-2016 (Carbohydrates: Ca (H:0)n ‘Monosaccharides a ~o 1, goneral Toma (CHO = wg 4, | 2 havea carbonyl (C=0) aroun A YT“ 5 small size an have mule hydroxy! (OH) groups Ary atl. ‘Sonne H bonds with water snd nonce realy soluble in water and easly transported in animat and PLY ie plant wansport systems re ee 4. sing stuctues extbia- and f-feomerism (a~ OH gp at Cts below ing and on opposite side of CE glucose B glucose fd BOM rp at Ct Is above fing and on same side as C8) (note: You must know ow fo draw a and | 5. areal reducing sugars Balucose meteculs) 6. eg glucose, galactose and fructose. Dissccharides Features, 1. are mada up 12 rmonosacchardes joined by a glyeostdc bond formed betwoon iwo moncsacchandes by a condensation reaction hat elves the loss ofa water molecule. 2. canbe split inte ther component monosaccharides is va hydrolysis reaction where, wih the addition ‘of one molecule of water, the glycosidic bond can be broken 3, many byroxy! groups extending Out ofthe ing ‘Ser H bonds wth water and henca readily soluble in wator and easily ransportad in animal and plant raneperteystoms 4, allare reducing sugars except sucrose 5. eg Suotose = goose * fucose | fucose + ghicore ‘dhcove + galactose Features 7, general ormula{ wee 2. sre made up of many moncsaccharides joined by glycosidic bonds formed between them by ondonsation reactions which invoWe the loss of water molecules. Function — Plant storage polysaccharide “nimal storage poysacchaide | Plant structural poyssctharde ‘Slored as granules in chloroplasts ‘Sloted in Hver and muscle cols | Coll walls of pent cols Mado up of e-giueose monomers Made up of a-glucose monomers | Wade up of f-glucose monomers in amylose: at ‘monomors In amylopectin: 1-4) glycoside bond links monomers within a branch and. a(t) ‘lyeosidie bonds links monomers at branch 4) glyeosiah Bond Wis | a(t-4) glycosicic bond links monomers within @ branch and ‘2(1-8) glycosidic. bonds. Inks ‘monomers at branch points B (td) alycosiaic bond ‘monomers a molecule Tis points _ — - = ‘Oneriaion of | A ghucose unis fr the Gham have the same | Al glucose units nthe chain Rave | Alternate glucose unis rotated 180° ‘monomer orlentation _| the same orientation with respect to each other ‘Sirudure of each | Amylose i a helical” molecule while | Helical and branched malocule,| Long straightlinear chain molecule “amylopectin isa helical ‘and. branched | like amylopecin, bul more _| molecule ‘extensively branched ‘Bands Between | No interchain Fiyarogen Bonding No nferchain hydrogen bonding | OW @foups projecing outwards Te molecules both “iections alow interchain | hydrogen bonding _ Macs ta microiei fxration ow the siructures of starch and giyeogon make them good ‘STORAGE molecules How the structure ofcaluiose makes ira good ‘STRUCTURAL molecule Substrate to obtain ATP. 2. Comprice of haces. {can pack many subunits por unit vot Hence they are insoluble in wator ‘unalocied by Dee presence 5, Amylopectin and glycogen are branched 7 Large maiecile ade up of many a-glucosé monomers Hence itis @ hoge energy store as # can be hydrolysed to yiels many glucose molecules that can be used as a respiratory b. in which most OH groupe. aro involved in Intramolecular Donding fow OH groups avallable for H bondi 7 Adjacent glucose unite are inverted 160° with respectio each other ‘and hence form a linear molecule with fre OH groups projecting out in both ‘rections which can hydrogen bond with OH groups of other cellulose ‘molecules lying parallel to and frm microfibis “Thus te microti have high tonsil strength ume 2.As a macromolecule, celulose has few OH groups available to hydrogen ‘bond with water as most are nveved in interchain hydrogen bonding. Thus nly the surface of the mierofori has OH groups that can hydrogen bond ‘with water. Thus ealldose & Insoluble in water and the YW of cals are ‘unaffected by ts presence. with water, ‘and the Ww of cals are 23. The meshwork of icrofris that form the coll wal have a porous structure they have multiple branch ends which hydrolic enzymes can ‘work on, Thus more guicase molecules can be released and ‘more. ATP can bo gonerated by respiration per unit time. » branching optimizes packing of many subunits pec unt velmne ‘and hence more eneray can be stored per unit volume ce branching reduces. the accessibility of water and thus feduces the solubility of the moloculo. Thus the Ww of calls ‘210 unafected by ther presence 4 ‘and hence makes the cell wal a'freely pormeable lo water and slices and allows movement of ‘subetances in and out of cots ». strong and rigid and prevent the plant eels fom bursting due fo osmotic ‘sess, Cotulasos that hydrolyse cause are found in very few organisms. Thus cellulose cannot be hydrolysed and used 95 a respiratory substrate and I good structural molcule } Prapared by: Wire § Nai & Wire Wong SH “Rates Instation (55) _‘alalar Fanetions _—Teaibchyarates Test Procedure = ‘Observations and Deduction — [ Benedict's Test | 1. Place 2 cn of fest sokiion ina tet tube, Presence of reducing sugar is Indicated by Tormation of BRK red for Reducing | 2. Add equal volume of Benedict's reagent. reciptate Sugars 3. Shake the mature "colour of tral saluion depends on amount of reducing sugar ‘4 Heat itby immersing the tube in boing water bath for | present testis semiquantitative) 344 mintes. > varies from gieea io yllow to boi to bck et ‘eat for Non- | TTa nogatie rel for BanedicPs tects cbisined Tortie | Presence of non reac sugar wicated By | Reducing test soliton, then ‘+ Abiue solution remains when Benedt's ests frst cared out. ‘Sugars 4. boll equal volume of test soluion wih divte | + After acid hydrolysis, Benedict's testis camied out again | hhyirchlonic acid for about + minute to hydrolyse | ” “> colour offal skin depends on amount of sugar present | saccharide fo monasacchardes 2, cool contents of ube 3. neutralise aciic content with sodium bicarbonate solaon 4. carry out Sonedits tes or reducing sugar _ Todine Test for [1-~Add few drops of iodine solsion to 1 ca of fat | Presence of sarah Wicd By Bus Bac coloration ‘Starch solution (ora ploce of test specimen). ___| 2. Ghserve any colour change Prepared by: Mrs § Nair & Mrs Wong SH Storagestructures fiolastide) f containingstarch 7 granules ina potato Amylose (unbranched) 4 tubercell tee ee hmviopectn g Saeaes Py emcee noone (a) Starch 4) gence ofrGv ionih (6) Cellulose BGcose birkiok Oke 5 -scooen senna oan Cellulose motecuile (unbranched) | OE Hydrogen bonds SOx resdnincvns oof NOON aos instuaion (7%) zCater Funan Er > Lids have a much smaller proportion of oxygon to hydrogen and carbon compared to carbohydrates. + They ae insoluble in water 1 Can be classified into: tiglerides, phospholipids and steroids Tiger Bhosphopid ‘Siradure | Consits of three ong non-polar, Rydrophobie hydrocarbon tals accociated wid a glyeerol backbone. Formed when 2 kinds of smal molecules join together + alycerol (© alcohol with 3 carbons, each bearing a hydroxy group + fatty acias ‘2 long hydrocarbon chains with a carboxy group (-0oH) © hydrophobic a nature as they have non-polar Hons inthe hydrocarbon chains (© maybe saturated or unsaturated Consists of two Taig” fienpolar, tiydrophobie. hydrocarbon tails attached toa glycerol backbone (not tree) “The tied hydroxy group of the glycerol is joined toa negatively ‘charged (not polar) phosphate group. Addtional small molecules, Usually charged or polar canbe linked tothe phosphate group to form a ‘variety of phosphotpids (NS: the charged phosphate head is not on the same Side ae the non pot, hydrophobic hydrocarbon tal) ‘Condensation readhons Take place i the formation of Both, though th phospholipids, a phosphate group is added in place of a non-polar, hhydrophobie, hydrocarbon chain ofa fatty acid molecule In triglycerides: Three non-polar, hydrophobic, hydrocarbon chains are Joined to a glycerol backbone by an ester linkage. An ester linkage is ormed betwoen a hydroxy group ‘acid joined tthe glyco. ‘OH) and a carboxyl group (COOH) via a condensation reaction, One water molecule is ramoved foreach fatty Properties | Nonspalar “Kmuphipathic a2 they have both hydrophilic and hydrophobic resions ‘molecules, je they are hydrophoble, and therefore are | « hydrophobic. hydrocarbon tals. are. excluded fom water. wile Insoluble in water. hydrophilic charged phosphate head (and its alachments), will Interact with water molecules + Inwater, they sa-assemble Into aggregates such as 2 phospholipid bilayer or moele which has a hydrophobic coro that Is shielded from water. Function | 7. Exoelient energy store G8 KIg") 7" Miajor component of phospholipid bilayer of membranes of calls (@ gram of fat stores more than twice as much energy ‘38 gram of glycogen or starch (per unit mass) and hence is a compact energy store) + a5 it has @ high proportion of C-H bonds in hydrocarbon chains ffom which energy can be released daring oxidation (main role) + a5 it is insoluble, and thus will not affect water Potential of cel nor be easily ransported cut of cal 2. Production of metabolic water + Oxidation of triglycerides produces metabolic water. Parteulrly important for desert animals. 3. Protect internal organs 4 Thermal insulation ~ by subcutaneous fat (the layer of {ot beneath the skin. Improve buoyancy Reservoir for storage of fat soluble vitamins ‘and organelles which acts | + as a barrier to polar and charged moleculestions as its hhydrophoble core has a very low permeabilty to polar and chargec molecules + as 3 boundary between the inracelar & edrecaular aqueous ‘environment and allow compartmentalization within cel Msjor component of liposomes + Artifical vesicles surrounded by a phospholipid bilayer that can be ‘sed to carry therapeutic DNA into a target cel ‘Propared by: Mrs S Nair & Mrs Wong SH Rafies Institution (Vr 5-6)‘Folate Fancitons —— 20182076 [* Sieroias |" (a) Properties of stroids e.g. chotesterot + loll in water and sli nrg overt. * Cholestr| asa charaori fur fused ring suture andi tage hrophoblc. Like phospholpds, tis slightly amehipahi, having 8 hydrophilic rydrony (OH) grou andthe hydrophobic np stun, © fe hydrony group of choestrlinteracts wih phosphate heads of phospholipids whi the hydrophbic rng structure intra wth the ‘hydrocarbon tas ofthe phospholipids via hydrophobic Interactions (©) Function of steroids eg. chotesterat + Cholesterol regulates-membrane flusity ie, & stabilises membrane, The membrane is preventéd frm being overly fluid at higher temperatures as cholesterol restricts phospholipid movement © _The membrane s prevented from being overly frm at iower temperatures as cholesterol prevents lose packing ot hoops Emulsion Test for Lipids tthe test sample a solution: 1. Aid 2 em” of ethanol fo two drops of test sample Ina test tube. Mix well and allow to stand for 2 minutes, 2. Decant the ethanol into another test tube containing 2 em of water. ifthe test sarppe is 2 soe: 1. Add 2 em of ethanol to ground test sample in atest tube. 2. Micwel to dissolve any pid if tis present and alow tt stan for 2 minutes. 3._Decant the ethanol into another test tube containing 2 en of water. ‘Prosence of Hpids indicated by. *+ A homogeneous (or dest) sohtion is formed with ethanol and an emutsion was formed when water was added, W fpids are absent, a dear solution Propared by: Mrs 5 Nair & Mire Wong SH Raffles institution (YF 55) Es —zProteins 20152016 + Amino Acids — Basie structural unit of proteins "Structure © consists of an carbon atom covalently bonded to 4 groupe, 1) hydrogen atom. 2) amine group (-NEt), 3) carboxyl group (COOH), 4) variable R group + Properties of amino acids (© Classified according to thei Rgroups as polar, charged or non-polar ‘© Exist as zwitterions in sotton - cary both postive and negative charges. © Actas butfers > Can donate or accept H, therefore able to act as an acd or as a base — amphoteric > Essential in biological systems ~ sudden change in pH could adversely affect performance of protein like enzymes. = Polypeptides ‘Amino acs are joined by a poptide bond via a condensation reaction with the removal of one water molecule, + Further addition of amino acids resus inthe formation of ainear polymer called a polypeptide ‘© Regularly repeating part, the main chain, is referred to as the backbone, © _Vatiabie part comprises the distinctive variable R groupe * polypeptide folds inte @ specific three-dimensional shape / conformation *+ The nucleotide sequence in DNA determines aa sequence in polypeptide which determines types and locations of R groups which determines group intoractions which determines 30 structure and function of protein, > A evols of organization inthe ctudture of proteins ‘+ Refers to the number and sequence of amino acids in a single polypeptide chain + Linear structure maintained by peptide bonds + The sequence of amino acids (and their arouns} in a polypeptide chain determines the type and location of chemical bonds/interactions, and hence the 3D conformation and characteristics of a paricuar * Refers to the spatial arrangement formed by regular colling or pleating ofa single polypeptide chain ia one direction. + Maintained by hydrogen bonds at regular intervals © Formed between C=O and N-H groups ofthe polypeptide backbone. © Regroups are not involved + Erarmples of cocondary structures: o ahelix + Made up ofa single polypeptide chain which s wound into a colled/spiral structure. ‘A hydrogen bond foms between the C=O group of one amino acid residue and the N-H group of another amino acid residue four amino acids away along the backbone ofa single polypeptide + There are 3.6 amino acid residues in every turn of the hel © Bpleated sheet +" Two or more regions/segment ofa single polypeptide chain lying side by side are linked together by hydrogen bonds ‘+ Alnydrogen bond forms between the C=O group of an amino acid residue on ‘one segment and a N-H group of another amino acd residue on an adjacent ‘segment along the backbone ofa single polypeptide Hydroptiobic inaction ‘ Ghains may run parallel (same direction) or anti-parallel (opposite directions) ‘elwvéen hydrophobic R «__ Forms flat sheet which becomes folded ‘+ Stucture formed by further extensive folding and bending of a single polypeptide ‘chain, giving rise fo the specific 3 conformation ofa protsin + Maintained by al 4 types of interactions © hydrogen bonds, fonic bonds, hydrophobic interactions and disulfide bonds 0 formed between R groups of amino acid residues + Refers to the association of two or more polypeptide chains into one functional protein molecule + Maintained by all 4 types of interactions ‘© hydrogen bonds, ionic bonds, hydrophobic interactions and disulfide bonds, © formed between R groups of amino acid residues of diferent polypeptides + Constituent chains ofa multimeric protein can be identical or different Prepared by: Ws Nair & Mis Wong SH Fates istution (175) 7‘Cellutar Functions Bory Proteins = 2015-2076 ord {eS yon soon) 2. Each subunit is arranged so that most of its hydrophilic amino acid side chains are on extemal surface while ts hhydrophobic amino acid side chains are buried in interior 3. The 4 subunits held together by intermolecular interactions {formed between R groups (hydrogen bonds, ionic bonds and hydrophobic interactions). No disulphide bridges. Baample ‘Structure Function Hacmogabin | 1. Haemoglobin has @ quatomary siacuie made up of @] Dre" of haem group binds Temporarily w Oy, ST TE (Globular protein) | polypeptide subunits: 2 a-globin subunis and 2 p-globin | molecule can carry up to 4 Ox at atmo forming Hranspots Subunits, Each subunit fs made of globin polypeptide ‘and-a | _oxyhaemoglobin ‘oxygen inthe ‘rosthetic (ton protein) component called haem group. Each blood hhaem group consists of a porphyrin ring and an iron ton wesw Ormincses |) {FE,) : ‘Thus haemoglobin 4s soluble in an aqueous environment, can be transported and carry O. fom lungs to tssves vice versa ‘PAs a result binding of one oxygen molecule to one haemoglobin subunit induces a conformational change in romaining 3 subunits so that their affinity for oxygen increases. This is known as the “cooperative binding of ‘oxygen. -FCotagen (fibrous erotein) > ancseental, ‘component of connective tissue Inthe burman body. TA collagen molecule (aka tropocollagen molecule) Consists ‘of three helical polypeptide chains (not a-helices) wound ‘around each other ike a rope. (has quaternary structure) 2, Each chain contains about 1000 amino acids and contain a ‘repeating sequence, usually a repeating tipeptide unit sglycineX-v, where’ X is usually proline, Y is usually hydroxyproline. ‘The tropocallagen molecule can form a compact coil 3s. almost every third amino acid in each Polypeptide chain is a glycine, the smallest ‘amino acid. This allows i to fino the restricted ‘space inthe canter of the triple het. 3. Extensive “hydrogen bonds fom between ‘residues of the polypeptides, hence interaction with water molecules are limited. 4. Adjacent tropocolagen molecules are arranged in a staggered manner 5. Crossdinking (involving covalent bonds / involving lysine residues) of adjacent {ropocollagen molecules results inthe formation of fri ‘2 Bulky and relatively inflexible prone and hydroxyprotine Fesidves confer rigidity on the molecule, ‘Pinicreases tensile strength (abit to resist snapping due to stretching) and increases tensile strength and makes the molecule insoluble in water ‘Staggerediovertapping arrangement minimizes points ‘of weaknesses along fibrils ‘>Greaty increases tensile strength. 6. Bundles of foris together form large and long \) | PLarge sizeof coltagon makes i insoluble, an important collagen flres, Property for a structural molecule Fibrous protein ‘Globular protzia _ ‘Wade up of on ge chains formi ‘straight fibres. | Wade up of ide chains folded into roughly spherical shape. Tt large and ianted in ts abisy to form hydrogen bonds with water insoluble in water since extensive hydrogen bonds already formed botween residues in diferent des. ‘Less variety of amino acids are used to construct he protein” te, consists of repetitive regular sequence of amin acids. (eg tipeatide, aly X-Y repeats in collagen) Polar R groups are exposed fo water molecules in the aqueous fenvironment->Soluble in water since these polar groups can form sdrogen bonds with water molecules. ‘More varity of amino acids are used to construct the protein le. consists of non-epetitve amino acid sequence Lenath of polypeptide may vary slightly balwean two samples ofthe same protein, yet protein is stil functional Length of polypeptide is always Identical batwosn two samples of {the same proten, of else protein may not be functional Example | collagen haemogiobin Test Procedure - “Observations and Deduction: Biuret Test [Y. Place 25m of teal soktion na testlubo Presence of protein indicated by a 2 Add equal volume of §% NaOH solution ‘Purple colour developing slowly. A test for | 3. Shake the micure well eptide bonds) | 4. Add two drops of 1% copper sulphate solution, shaking well after each drop. Denaturation of proteins: ‘3D shane of a protein may be changed by: (a) Heat (afect hydrogen bonds, hydrophobic interactions) (b) Acids/Atcals(afect hydrogen and ionic bonds) (6) Inorganic ions (affect tonic bonds) (4) Organic sovens (affect hydrophobic interactions) (e) Mechanical forces (affect hydrogen bonds), NB:_1. Peptide bonds not affected. 2, Strength of bonds: hydrophobic interactionH bonds" Effective collisions fake piace between the enzyme and substrate > _ Resulting in the formation ofan enzyme-substrate complex. = “Amnino acids residues that make up the enzyme have different fancions: ‘Contact residues found in the active site —help to position the substrate inthe correct orientation via weak interactions such as hhydrogen bonds, ionic bonds & hydrophobic interactions. 2. Catalytic residues found in the active site — act on bonds inthe substrate and help to catalyse the conversion of substrate to product 43. Structural residues interact with each other to maintain the overall 30 conformation ofthe protein 4. Nonessenta residues — found on sutace ofthe protein — no specific function. ~ Enuymes speed up metabolic reactondlallows metabolic reactions to proceed at moderate temperatures by lowering activation energy (Ea) of the reaction, through: 1. proximity effects — temporary binding of substrates in close proximity inthe enzyme active site increases chances of a reaction (vs ‘depending only on random colisions between reactants in ‘the absence of enzymes) 2. strain effects ~ stight distortion of substrates as they bind to enzyme strains bonds in substrates that need to be broken for products to form 3. orientation effects — substrates are held by enzymes in their active sites in an the correct orientation such that the bonds in Substrates will be exposed to chemical attack 4. microenvironment effects ~ enzymes create the appropriate microenvironment for a reaction to occur €.9, hydrophobic amino acids in enzymes create a water‘troe zone that allows non-polar reactants to Teact more easly ‘5. acid-base catalysis ~ R groups of acidic and basic amino acids in enzyme ‘active sit facilitate reaction between substrates Hnce there willbe a greater proportion of substrate molecules with energy ‘greater than the activation energy. allowing the reaction to proceed faster than a uncatalysed reaction wd Vee peal eno [enon aren cu > Enzyme cofactors 1. inorganic fons (e.g. magnesium ions in PCR) “> mould enzyme or substrate and allows enzyme-substrate complex to form more easily 2. prosthetic group (e.g. haem group of cytochrome oxidase in electron transport cain in inner mitochondrial membrane accepts electrons from cytochrome C and transfers them to oxygen to form water) > permanently bound to enzyme > ransfereatome/chemical groups between active ste of enzyme and another substance 3. eoeraymes (¢.9. NAD transfers electrons in certain redox reactions in respiration) ‘> are organic molecules that are required by certain enzymes to carry out catalysis > they bind tothe active site ofthe enzyme and participate in catalysis but are nat considered substrates ofthe reaction > function as intermediate carters of electrons or spectic aoms that are transferred in the overall action Prepared by: Mrs 5 Nair & Mrs Wee SH Rafiles institution (17 5-6)‘Cetfutar Functions: 2015-2046 ‘Measuring rate of produc! Yormation Measuring rate of disappearance of substrate Rate of © production decreases with time 2H0:——> 2.0 +0, Stach > edueng sugars ‘catalase anylase ‘ode Example 1) boinc i presence of iodine > incomplete digestion of starch 2) brown in presence ofiadne > compe cigeston of starch Deondent | Vous ot varie" _| Volume of, evoWed per unt tine / over a xed period of ime | Change in ictnsy of bv back cxlouaton of sarchioine compen ec unl ie over a fed peridot me a Concntatan af aubsate and anayve Rap anata Coneaiation of substate and rej Rap onan variable _| Alter conditions that afect an enzyme caaiyeed reaction, | Allether condor that ales an scyme eaaied action 9. pH, a. temperature hap constant temperate kept constant Eipamental 2 setup Dropper Drops ot iene amyiase wnte te | ad sarch Note: Deliver tube may be attached drecty to ga syringe 1. Add enzyme amyas) to starch and tat th stopwatch immediately 1. A enzyme (alse) to Oe, mic and stat the 2, Aad ed tie inten, varsered a dopo the eacion mre stopwatch toa white tle wie ocep of acne Procedure | 2 Oz evolved can be measured bythe downward 3. Inthe presence of stare, iodine ums om ylowish brown o oe displacement of water in a graduated cylinder (as shown blue-black hove) or using a conse gas syringe. 4 Intonsty ofthe be back colouration can be measured using a 2, Recor volume oO; avlved at fed te intervals caloerter 5 Use a standard cure to convert the cledeter ean to starch concentvaion : fond Graph re ee pate Int rate of racon = Gradient of curve a tne 0 see Ini ate of reaction = Gradient of cue a tine 0 see Intnsy of blue lack colouration / concentration of starch decreases I Volume of 0; evolved increas wi time wit tne Rate of change in intensity of blue black colouration / Rate of decrease of sarch decreases with te + To investigate how factors lice pH, temperature, fenzyme] or (substrate) can affect the rate of reaction: © Vary independent variables e.g. pH / temperature enzyme] [substrate] (© Keep all ther variables constr © For each condition, plot a graph of amount of product formed vs tne and obtain te inital rate of reaction, © Plota graph of rate of reaction vs the factor investigated (lt / temperature / [enzyme /(sutratel) Notes Prepared by: Mrs S Nair & Mrs Wee SH ‘Raffles institution (Wr 58) z‘Coliviar Functions Enzymes: ‘As temperature. ncroases, IKE. of enzyme and substrate molecules increases > Frequency of effective collisions between enzyme and substrate molecules increasesses, 3 Rate of enzyme-substrate complex formation increases. Number of cubstrate molecules with sufficient energy to overcome the activation energy barrier and form products increases and rate of reaction increases, ‘Temperature coefficient, Qi = Rate of reaction at Oo+10)°C Rate of reaction atx°C When Qu=2, for every 10°C rise in temperature, the rate of reaction’ product formation doubles ‘Beyond the optimum temperature, KE. of enzyme and substrate molecules continue to increases intramotecular vibrations increases hydrogen bonds, ionic bonds and hydrophobic interactions that maintain the 3D conformation of the ‘onzyme are disrupted ‘(Covalent disulphide bonds are harder to break and thus can withstand higher temperature. Hence enzymes with higher optimum temperature tend to have a larger proportion of cisulfide bridges ‘or more intramolecular interactions.) > Specific conformation of active ste is lost > Substrate no longer complementary tothe shape and charge of active site and cannot bind tot | 2 Rate of enzyme-substrate complex formation decreases and rate of reaction decreases. CN 075-7076 Etiect of oH ‘Atoptimum pH, ‘> Conformation of enzyme active ste ie most deal for substrate binding and rate of reaction is highest ‘As pH doviatos trom the optimum, "> Excess H’ of OH ions affects the ionisation of the R-groups of the amino acids residues: tonic charges on the basic (eg. NH) and acidic (eg. COOH) R-groups of the amino acid residues are atered > Where excess 1" reais fn -COO' groupe becoming COOH and excess -OH resutts in NHS’ becoming Nit > Thus lonie bonds and hydrogen bonds that maintain the conformation of the enzyme active site is disrupted Thus the interaction between substrate and catalytic residues inthe active ste of enzyme is disrupted > Rate of enzyme-substrate complex formation decreases Rate of reaction/product formation decreases (Note: ithe change in pH affects the charges ofthe R groups of the (1) catalytic residues inthe active ste, the catalytic activity of enzyme may be lost (2) contact residues in the acive sie, this may affect the temporary Binding between the fenzyme and substrate and thus no enzyme-substrate complex forms. (@) structural residues, the tertiary structure ofthe protein and ts active site can be affected and this would denature the enzyme.) Rate of reaction coptenum pH ‘optimum pH cof rypsin 6 8 10H Effect of fenzyme} Ina, when fenzyre] is tow, a fenzyme] increases, > Frequency of effective collisions between enzyme and substrate molecules increases Rate of enzyme-substrate complex formation increases and rate of reaction increases Allinear portion of graph, [enzyme] i limiting > Increasing enzyme] wll resut in a proportional increase inthe rat of reaction [At curved portion of graph, enzyme] isnot the only imiting factor. Some other factors also limiting At the plateau, [enzyme] is no longer the limiting factor (Other factors are limiting) Increasing [enzyme] wl not affect the rate of reaction Effect of substrate] Inia, when [substrate] is low, as substrate] increases, > Frequency of effective collisions between enzyme and substrate molecules increases. > Rate of erzyme-substrate complex formation increases and rate of reaction increases as active sites of enzymes are readily available and substrate concentration i limiting Beyond a certain fsubstrate}, >A active sites of enzymes are saturated with substrate at any one point in ne > [substrate] Is no longer limiting and enzyme concentration is Constant(graph plateaus) and reaches maximum volocty (Vu) ‘Michaelis constant (Kim): (subetrate] at which reaction procoeds at half ts max. rat > Low Km= high afnity between enzyme & substrate High Ki — low afinity between enzyme & substrate fate of reaction te ‘Subetrale concentration Maxie velocity Maximum velocity Michaeis constant Prepared by: Mrs $ Nair & Mrs Wee SH Rafiles Institution (158)Cellular Functions Enzymes ETE ‘Allosteric Inhibition / Activation Tatibior [Activator binds to ctive site ‘Site other than active site ‘Allosteric site Shape and charge of inhibitor 7 Similar in conformation and charge | Not similar in~ conformation and | Nat: simlor i confomalion and activator fo substrate __| charge to substrate charge to substrate ‘Sttuctue of enayme **Can consist of subunit with T|"+ Usualy a 1 subunit with Tadive |» Mutimeric enzyme wilh muRpie active ste se ‘active sites © Presence of cooperative oR binding of substrate to active site '*Can be a multimeric enzyme with + Has mutiple allosteric stes ‘multiple subunts, each with an © But, binding of 1 inhibitor active ste Iacivatoris sufficient to inhibit activate the actvty. of ‘the enzyme Efecto inhibitor 7 activator “on ['sinibtor is structurally similar to | » Inhibior ls not structurally | > lahbtow AGWvalor& not azure X the tate ofthe enzyme: | substrate & hence binds |" similar substrate & hence binds | "structural ster saterate & catalysed reaction reversibly 10 active site of | toa site otherthan the active | hence binds to allosteric ste ‘enzyme site > This results in conformational |? Hence intbitor competes with |->This resuts in a conformational | ~ change enzyme Substrate for active ste of | change in the enzyme active | >Binding of anbior stables enzyme site ‘enzyme in an inactive state > This reduces the availabilty of |>Tnus substrate cannot bind to | ‘Thus the rate of reaction ses active sites for substrate | active ste Binding. of activator stabiises binding > rate of reaction Ves enzyme in an active state L. > rate of reaction decreases “Thus the rate of reaction ses Eifect “of [subsiate]_on the | «At high [substrate], substrate ie | + Tnhibtor binds o ite other than Inhibition ‘more likely to bind active site |” active site and changes the than the inibter to form enzyme- | conformation ofthe ative ste substrate > Hence the inhibitor effectively | Hence the same Vmax can be |” decreases the available ‘reached at high [substrate] enzyme] as itforms an j> Thus the effects of inhibition | enzyme-inhibitor complex can be overcome at high | Hence the effects ofthe [substrato) inhibition cannot be overcome by increasing [substrate] Graph demonstatingefieaof ‘The enzyme freely oscilates inhibitor / activator between the active form and the inactive form, > When the activator binds to the enzymes, the active form is stabilized > When the ihibtor binds to the enzyme, the inactive form is stabitzed > Vmax decreases |S Km increases 5 Kin remains the same pst - ae a fe ‘End produel inhibition ‘eg, Symthesis of scieucine from threonine Regulation of a metabolic pathway by the end-product ofthe pathway >End-product can function 3s an allosteric itor to an enzyme | Intl subse —_+ wemcite A———_temediate 8 ——> Entort Finding fo te octet and Emmet Ennme2 Emme 3 Prevent further synthesis of the (reonine deaminase, ‘an allosteric enzyme) Fe Isoleucine binds to allosteric ste of enzyme > active ste of enzyme changed. no longer binds To threonine ‘Note: Athough enzyme ihibiion can both be reversible & WrevOTSibe, we are more concemed wil reversible InhibRors Wh our slabus Product. Prepved by: Wes 8 Nair Ws Woe SA ate ton (5) a“Gofular Functions Call Siuctare 20167016 * Imereonversion of units (max, jm, nen) "10° micrometers (un) Er errr er Semester Nucleus Sierra + Prominent spherical orpanelc in ceuraryotic cal + Suounded by a nuclear envelope (a ‘double membrane) which fs perforated with pores & continuous with RER + Contains the nucleolus & chromatin Uses graticae and siage micrometer to measure calls and be familiar with units (milimetre, mictometre, manometer aed iy CoM etUaICS recognising the ceremony ‘+ To contain th hereditary material + Tocontrol cell activities by eymthesicing ‘MRNA which willbe vansiated hia. Proteins which are needed Inthe col 1 Nicieotue rucleus + Contains ange amounts of DNAJRNA & protein ‘Non marbranous, spheres wii + Tosymthesise RNA, a component of fbosomes, + Assembly of large & small ribosomal ‘subunits using RNA synesises in fucleolus & proteins exported fon ‘oplasm INB: Substances pass between nucious & ‘Chromatin ‘evtoplasm via the nucear pores. hey are + Heredtary material of he call 1) "Wee nvdeotides & enzymes (Yr ONA ill cs pant sicapeneaiisaas saan replication & transcription), proteins (co make up bosomal subunits) wich enter the ‘called around histone proteins ‘+ 2iypes of chromatin are present ‘cleue 4. Euchromatn ight stained, 2) MRNA, RNA and large and smal ribosomal eae subunis which leave be nucleus) ee ee 2. Heterochromatin (dary stained, transcriponaly inactive, usualy found along the edge of nteus) = Consists of the RER & SER ‘Smooth ER ‘Rough ER (RER) + Anetwork of membranous fatened 2 | Zoi Has besomes attached to the outer + Totransport of proteins which are synthesised bythe ribosomes on ts Srface tothe Gol apparatus via ‘wansport vesicles + Toallow proteins to fold into the native ‘conformation inthe cisternal space & ‘iycosyiate them Ee setae ttirctene | 2oeerom perm = Smear SEZ SS oe OS0S ‘Smooth ER (SER) {Tho RER and SER together act asthe ‘membrane factory of te eal by aang + Anetwork of membranous tubular sacs ‘membrane proteins and phospholipids tots own | called elstornae ‘membrane + Lacks ribosomes on outer eurace 2.Proteln channels onthe RER surface ‘= Hold the ribosome In postion + Aon the entry of polypeptides synthesised on ribosomes on the surface ino he umn (Singular: cisterna, Purakeistorae) ‘To synthesise lipids and carbohydrates + To detoxify drugs & poisons (Thus SER abundant in ver > Werbrane bound fattened sacs caled cetera & assoclaed Goll vores + To alycosylata to proteins and wpe to {orm glycoproteins and gyeaipise ‘eepectvely + Tomodity existing glycoproteins and lycolipid by modivingcieavng the ‘sting sugar chains ‘+ Tosort and package proteins int diferent vesicies and target he proteins lo diferent pas ofthe cel or for secretion + Totarm tysosomes + To-synthesises polysaccharides such as bectn wich is transported in vesicles to re coll membrane. ‘ra face = + Consist of Yorming or‘ face ou 2S Golalvesices where new cistemae are being formed wes bison of vanspoa vekios tom ER Ba'maturing" of trans face fom S$ of atone. which Golgi vesicles continuousty bud “Sse a iste p 7 Wenbraneus 63 cotinine srzymes ING: The hyrotytc enzymes work bestin the acidic environment of the yeosme. Thus #2 Iysosome buss, the enzymes are not voy ‘atv asthe eftosol has 2 neutral pH, However, tiny ysesomes burst, ten the cll wil be destroyed OQ aveneae + To digest material engul bye cal + Toseltdestruct a cel ater its death (autotysis) “Pepuredy: es Sevan Ma ates nso (79)‘Celular Functions Geil Seuctare PILE Organs [Beserpon Fina NE Secon Sanne eeT founded by Soule menbrane Aerobie resprationte generis energy la =a "qe otter membrane cement | telomaf ATE 2. eter membrane hay ‘Niner mecha mambrae i ihly Convauted winnings called tded 8 hence bereses sacs chnae dion encative posphoraton A + Betweon te membranes the 2yiitoconatal mass he tof i ae intermembrane space nk recton& te Krebs yee PTT Uiitttmane | © Gikoepreee ri som ue marc a [Eee Coelaiog ecu ONAL 70S Soe /g% —L_jnememtraneseace | Siocomte:phoeehtsgrmuts & hE ‘enzymes for aerobic respiration are6ntate complex + AiPayetnase complxon er (appears as a stalked particle) membrane projects into matrix 7 Tens ape iui aneanded ya | > — Gps coin cheap out monrane ‘ont so energy chem entty aaa + Win tbe rons internal trough potorynet a ser ARETE seosomes mmombraneaystomwhichcoresisot | 1) Steolighependent reactors a fond sac cae thy (e eorice nonagce ax factor yates granu) & Pheiphoeprorain which acon fecrorna meta Bre thyaketd montane + Riurwann corps surounding te | 2) Steet ighncapendentrencSon (i. sana oa eo foto Gavin je wich oa nthe om ‘reutar ona, 7 taccomee, ato sriymea tar gle) IN: Uke bac, oh copa & Zkte | + Shorophytmoletee stood on | miochonda conan cas OMA 708 intorgranat aren 27880 |" te tyakotd membrane ‘osomes, This led tothe endosymbiont Samet anu TE eee naka | teary wichoroposes hee sions of he ‘roplet STI" membrane |” Tembrane project into stroma, ‘mitochondria and choloplasts were oxygen using Tonos potas an Dhoteynate pokanyoes especie, at tr gid by a scncial meatal or Deets rumen + Cont fa mal aarg Baba +A be ase po Ses 2 ACoimplex of protein & NA 1 ttsybe oundinaet ety tating n ‘amateur (405) the cytosol or bound to ER. forouer = mmemtrane ofrcenremretye she | INS: Free rosomes paiice poe that tg sunt 05) ERlecorteusw onthe mea’ "| Wncon' wan: tne Gyo whan bound trvelpe) ung barlato. The smat_| tosomes "eynhese pots meant fr Stage stu yom occ | Woeon io manbrne"peckag wihin ducal, cxpueles or secon ot 7 Kost of low ine made wp TS + Toes miele organising Se me tnaat {ipetsofmicrombules roto ides | QTC) ding eps frmaton hcl ft ov tage of tre protein tbat) each ‘iision | (yf 2 Renee tt 1 A 2 a ngntangies to each aber INB:1 Duta cat ey, he cotices ie 3 + Foundina agin cated he repli move oposte cds of he I han! “centrosome which is the microtubule Baie bape tied roars conte TOS ts tg ance he [J] eke mnt] Sond eeeareanoes snois each Sabu) trl vow oer annie plas crt ae absent) Tie endomembrane ostem coasts oe Rade enVEOpE, Oh GRIOIETE RGA TREAT aot eros: wis SER), CORT 2opeti (Gn), beosoes and vas ves ad he paste menos DNA sangre inthe mucus mRNA MRNA eaves the nos ihe mula pores INA is nae in poppies on he bosoms tte PER polpeptes ere bw en of be Ctma of he NER where tundegoce noeaion® anspor wide Puss of tom be RER ord Cary te poten tothe GA Sve es with ho fae of he Ga adie ps undergoes ber medion, sours and pace a Sector vestleconting the poten ba of om hear face of te Gh and be Yanepoed te and fe mth bs cal ste mama ‘lor he prot content te vesiiey exces, Microtubule dec the movetnent ef te bansjor veste tte GA end tw reeetoy ‘esis a cal setae membrane Expat and ditng ish BebwennFesSlalon avd agaation Reaotuon The rani dace wherby wo pnts can be separated ad ti be tinguished as wo pons. ‘tagamcaton: the core lo wich no wewed rages ger han he ssn, M tlegicaon: Lenn of rowing =X (WE: tale dion of eyepacepatcle undo Low Foner 0 oooeve) = Tm Length ot specimen ‘malet diion of eyeplece acu under High Pwer (ao ates) = Sum) (Vote vaway used's omc) Taner: Yon Draw lan dagems of asus ad calculate near magnifications of dewings inn mating wge ems: STAMP tea ring occupy 20 gen space 1 Fitemuntindude:plae teacion nana oepctnan, name ol ese / a magnitaon 09.1.5. of elena ct foie A inmotion fas Sars aly ool wa test fe Mogntteston | B:Propordo: 9. Cal wal camo be oo ick when dewing a plant cl Rms be poporona ihe est ofthe a. Rates Institation (Vr 68) z2016-2016 aa ee alyeolipide proteins & glycoproteins Pisa membrane or Call sare membrane Sours mc 3 ite hee a mossc model stucure ““ruif Coca he menbron is dynamic sce whee he potpolpis & proline ae alo move {ips can move tt iateraly& taneverel ip fo) wae proene mor larly ds weak Percns between he Bonolees) - ‘Moss teense eth random arama pots whe ebedaed ta hol ase ‘xvacetiar mati vcopatin } sycotnis Crectrate Sane lateral ee unt ror tts trot ese enn Freon poten os transmembrane chanel retin (evmee reg poten fas 2 ‘ cotaam treo pr tr mover ot z ‘cand ptr mooie fete ete enolate Compan | CRaraciisic of componente rae Coch poaprpa moe “AS hae cepOREATO cal mane Binyer™""" | “ie hast hyo negative eharged | 1) "Actas Douay tetvan he Poscahdr&wcaceirevonmant Dhoapate head tarot 2 ‘Aiowscompartnetttston ina Rona yerecrbon tale at siachesto | > nonce & rogues the movement of substances ib & out of he ctiest Soyeer bsetbone Theinembranee prevered fm beh oe maior onpeaties as hydrphobi't ring sracte hoketer! rovers the cove gaong poeple end. Nees “Thetydom|geuptcnseneclatoewin | peers sthieionknrltce the dyed peste heats ft + Cnt etal the i ye’ uo van er Waa rico Bhospolds wile et ots txt ao |" beweonte id hse dg icra el eer Srehydrphoti ore te mena raat] Sos art tansenbrone | “Fins a GRASS eRe RGIS, BS TRSDOT prone! {) Chane Protaine “Have danane bat ae herophotaswn_| sr taneembrane proteins nonpao) moptncasswh por | maybe gta nich ears ty an open alow eas of sees rosary) trthy can be dove a ponds eaten opts Ths resid be amphipetie the moveren af soles eg. wotae ued Cha nero > ay nal be ated. toms on ope stage fb et Sse of (Gs ancums econ he morae fms igh ical saute ‘ncaa 09 easorne 2 Gare retains he rate conomaos) + bide ote on onesie of be manure a aes te pti Trarspatacoss montanes ie wtttoacet, |” uannocs a conornalona change et sow esesr athe sloats spe : ‘o | staspnetetidect mentee eg gece torso sn re ro pr hal wat re ATP mow sola gana ‘maintain homeostasis inthe col ‘concentration gradient (rom a low solute concentration to a high solute ° iis at a tsiog Suen | The oove wo yes Srl se acess br he mevenet of charged St Mate a ith ae ea | 0 oe ino ncaa fhe move ol ha ove sro hte oem UATE we | Pro fg) and por unhuned elec (oy gee aay ec ‘East polis can pores Wo hae en he be 9) x te master of inie_andents | -Foncon a esymes (9 aceeetnestaze wich ond on pos ss pave cls So at inpass cn be | sranicmenbrane nye nearer sca) Soren -Finclonas receptor rtsins (omnes few spect and i salon, The fmalon feta ere ample leon ) ye secon of santead-amdas | rcohar sgt caccooe or Sel tcresica) aa fommones Beha -Funclonosaiteememrane scar ay a on-covatny bund lodstream to maintain blood givease | “to cyoskeloton (on cytoplasmic side) & extracellular matrix (on extracetiular toes) sat Sepa | Catena Twa 1a oa cna can wavy vee cana cE feninre pone: “uncon: arkersecopivon sa akc ecogaon and Gas | Catt hans aiocog aves ws | |” saecin hyeopri tats of membrane (et a ti alos cls be atached'a one nar oom ste and ons: Phosphate hea) ~Funcon oe receptors 9 fsa chema a hones Prepared by: Mrs. Selvamsni Nai ‘Rates lnstalvon (VF 56) zaller Functions - Geli Membranes 2075 2096 EAM 1) Membranes area partially parmeable barrier which act as @ houndary 2) between inside and ouside of ce () between organelle and ‘evopiasm (69. Golgt apparatus & cytoplasm) &(c) betw. comparinenis win an organale (eg. mochondial mate & intermembrane space), 2) Membranes alow for compartmentalisation which alow unique environments tobe formed or highly specialised acthes (eg ace envionment in lysosomes for hydrolytic enzymes to work) (0) Spatial separation of biochemical processes & thus thelr sequential operation within a cal (€.. protein modiication in RER and further protein mosiieaton, eorting and packaging in the GA) Gi) accumulation o ions to tigh concentrators (€.g-accumulaton of high concentration of "inthe intermembrane space of the mitochondria enable a proton gradient tobe estabshed for hemigsmosis) 3) Membranes act asa surface for chemical reactions to occur ina sequential manner “> membranes may have functonaly-clated proteins grouped together so that sequential biochemical processes can occur (€.. the thylakoid membranes of the chloroplast have eleckon carers & ATP synthetase for chemiosmosis lo eezur). 4) Membranes increase surface area fer chomical reaction (9. nner mifechondiial membrane ls high folded to hold moe electron transport chains and ATP synthetase) 5) Membrenes surface topography enable communication of cel wih suroundige + the unique combination of protens/ycoproteins glycolipids on surface of diferent ces enable (@) cell-cell recognition and adhesion so that tissue formation i possible, (©) virees to recognize and infect host cells and (©)}gands to recognized specie receptors so that signal traneduction can occur CNT Movement typeot | ATP across Aranspor | eane | Protein | SSpe* | Semeting to note gradient _ Diffusion [ne —| no | down, ‘Defson: Net movement of mics. or ons fom a region of high concentration toa Tego ofiow ‘concentration, down a concentration gradient. __| 2.9.0, cimuses from the ings to te blood Facltated | 50 yes | down ~ Trangport protein faciliate dfusin of substances tha ae neolubl a phoapholpids Bayer difusion 29.1) transmembrane hydrophiic channel proteins (e.g. aquaporins) 2) canter proteins (e.g. glucose transporters) 3) voltage gated protein channels (eg voltage-gated Na" channels) open & close when an _acion potentials generated in nerve cel a a a Denon: Ena (ATP) consuming transport of mics or fone across a membrane Hiciaha transport ‘Waosmembrane tanspor orctin against » concentration aradient. Requires ATP & vansports mcs. gers 8 membrane Energy is required because the substance ls moving against its natural tendency to dse in the opposite direction -€9. Na-K” pum (€g. n maintenance of polarised tate of neve cel) = Mow of each mic or oni inane direction (unike dision which e reverse) Baik ves [m0 | downtup |" Requires ATP but ol considered as acive ranspor as t does not anspod mic. aes a tansport ‘membrane throush a transmembrane anspor poten, (However, tis an active process) 2 types: ‘WExocytosis: Secretion of macromolecules (eg. waste material fo the exterior of he colby ‘sion of vesite wih the plasma membrane 2}Endocytests:Inflding of extension of cel surface membrane to form a vesicle or vacuole, tus allowing cal to aquiro maccomotoculos and partculato matter respectively. ‘Phagocytosis: slits taken ino el via avacunle(all‘eatingXe.g, white bood cols engull, bacteria ) byPinocytosis: lauds aken into the cl via vesicles (col ‘rinkng)e.g. human egg cel takes Lup nutens from surrounding folie) ‘Osmosis [no [no] awn ‘Detniion: Nat movement ot water For raion a igh walor poten oa region of ow waar Polenta! down a water potential aradient thu" a parialy permeable membrane. Water potential ofa soliton > tendency for water molecules to leave a soliton, In plant cots, water potent depends on: 1) he extent by which dissolved solutes lowors water potential Le. the solute potential 2) pressure exerted bythe col wall against the col surface membrane ie pressure potential Water potential of plant ct = Solute potential of cell contents + pressure polenta of cl well 7 We We ‘The St uritis Pascal (Pa), Water poteatial of pure water ls zero. This the maximum fr water potenti ‘Whon we add solute, (1) Ve becomes ve 2) concentration of solute increases Wen we add more solute, (1) 97 Becomes mere —ve {@) concentration of solute increases more Wen we add even more solte, (1) becomes even more —ve (2) concenvation of solute increases even more + Atincipientplasmolysis, w»=0. Thus wa « we > the plasma membrane just starts to pull away fromthe cll wal Net water movement occurs fom 8 region o high water potential io region of fow water potential down 2 water potential gradient. ‘Prepared by: Mr. Selvemani Nai Raftes talon (55) zGadular Functions Penne See ere Puede 1. Organello synthesis occurs in the Gs & Gs Phases 2, ONA replication occurs during § phase (SC "Chromatin threads condense. Each ‘Ghromosome i visible a5 two sister {chromatids joined atthe centromere 2. Synapsis occurs Le. homologous Cthromosomes pair up to form bivalents 3. Crossing over occurs between non-sister ‘chromatids of homologous chromosome pats, forming chlasmata (sts of ‘crossing ove). Corresponding segments ‘of nor-sister chromatids ae exchanged 4. Centiles migrate to oppeste poles and spindle foes extend from each pole Tokinotochores & metaphase plate ‘5. Nuclear envelope disintegrates, 6. Nucleolus disappears 11 Kinetochore microtubules align Romologous Pairs atthe equator in two rows with each ‘chromosome on ether sie ofthe equator ° ation of chromosomes of bivalents completely independent of tie ofthe other 1. Kinetochore microtubules shorten and homologues are led by their centromeres {0 opposte poles. Non-kinetochore microtubules elongate causing the 2 poles fo move further apart (emarmne 1. Each pole has 2 haploid sat of chromosomes 2. Chromosomes uncolt into chromatin 23. Spindle fibres disintegrate 4 Nuclear envelope reforms around the ‘chromosomes at each pole & nucleo EES OID daughter cole resut 1. Chromatin treads condense Each chromosome is visible as two sister chromatids joined by a centromere 2, Centriles duplicate & migrate to opposite oles. Spindle foes extend trom each pole to kinetochores & metaphase plato 3. Nuclear envelope disintegrates 4. Nucleolus disappears. (EES 1. Kinstochore microtubules align chromosomes atthe equator in one row ch 2 Kinetochore microtubules shorten & pull the ‘Sister chromatids (now called chromosomes) ‘centromeres first to opposte poles. Non- kinetochore microtubules elongate causing the 2 poles to move futher apart 4. Chromosomes uncoll into chromatin 2 Spindle fires disintegrate '3. Nuclear envolope reforms arcund the ‘chromosomes at each pole ofboth cals 4. Nuclecl reapp, NTA ‘4HAPLOIO daughter cols resut [NOTE Soe cts p weghave Lan yc, Searapemet creby ate went thre ro ‘opus Conroe ss NOT SPLIT ‘Cell Nuclear Division 2075:3076 's& the associated behaviour of the nuclear SRaae ere rennet eee te ees 1. Organelle synthesis occurs inthe Gy & Gr phases ‘condense, Each ‘chromosome is visible a5 wo ster chromatids Joined atthe centiomere aa. MEIOSIS: MITOSIS | 2. Centoles migrate o opposite poles & senda {ores extend fom each poe to ietochores & a@-— ‘metaphase plate . itt / | 3. Nuclear emote dsinegrates ‘meee ~/ i Ys) | Nuclots asappears pee A] | inne rete oe J at the equator in one row ay 41, Centromeres of each chromosome divide 2. Kinetochore microtubules shorten and pull the sister chromatids (now called chromosomes) centromeres firet to opposte poles. Non-kinetochore microtubules elongate ‘causing the 2 poles to move futher apart 1. Chromosomes uncolinto chromatin 2 Spindle bres disintegrate 5, Nuclear envelope reforms around the Chromosomes at each pole & nucleoli reappear ‘Animal cols: ell membrane invaginates ‘towards the middle, forming a cleavage furrow. Cell membranes join up and separate the 2 daughter cate Plant cells: Vacuoles appear inthe middle of the ‘coll They coalese to form a cell plate, separating the 2 daughter cols =| Contains one complete set of cvomosomes el conains half the numberof chiomosomes a3 diploid cel, contains one member of each homologous pair of comesomes: Le. one chromosome from either parent) 5 contains two complete sets of chromosomes 6. comesomes exist as homologous pals Each set of chromosomes is fom one parent is meant by homologous pals of chromosomes ‘> have same ength, centromere postion & staring pattem ‘> cary genes controling the same inverted characeratios at the Corresponding loc! on both members of a homologous pair one is of maternal orgin + one i of paternal origin Hence each member ofa pairis genetically diferent om each other 2 pair upto form bivalents during prophase I of meiosis ‘Thus although each member of the homologous pair may have genes coding {or the same charactersts (0.9. eye colour) at corresponding lock they sre ‘enetcaly different form each other es they usualy have diferent alles (63 ele for ble eyes & for green eyes, each of which have diferent nucleotide segener eact of aaa ‘ are the resut of DNA replication and thus have the same alleles ‘> sce genetically identical (before crossing over occurs between non- a OV ©® m romain eae mat meter By CC ie ELS tem e *Q: Whats the difference between chromosomes & chromatin? ‘Chromatin: Complex of DNA & protein (Chromosome: 1) Uncondensed form > a mass of long, thin, thread-ke fibres of chromatin, 2) Gondensed forn > chromatin that has been condensed by collng and folcing many mes upon itself & appear short thick, structures, ‘Prepared by: Mrs. Selvamani Nair Rates institution (¥r 5-5) 7Setar Functions ‘Gail & Nacho Division Be RiIS IIE ntsol of replication * Bang phase of trast mas, replication of DNA occurs by seml-conservative replication where both parental ONA strands are used as template for complementary base pairing + ‘This ensures that 2 gentically identical DNA molecules (ie, sister chromatids) form ‘+ During anaphase, separation of identical sister chromatids occurs when centromeres separate and the resulting chromosomes are pulled to oppeste poles ofthe cal This ensure even cistibution ofthe DNA inthe daughter cols which wil thus contain the same hereditary materialsame alleles! same NAY same base sequence// same number of chromosomes *+ Thus daughter ces produced during mitosis are geneticaly identical to te parents i. no genetic variation occurs. ‘These cels will have all the genes necessary for survival of the cellorganism and wil be faithfully inherited with every replication cycle so that he resuting cals can continue to function normally ‘> Thus mitosis allows for growth, repair & asexual reproduction which require the production of genetically identical els. (Le. cell are dones ofeach other) Explain no portance of mi *+ Mitosis isa form of nuctear division which resus inthe formation two nuclelfals that are genetically Identical tothe parents Le. mitosis maintains genetic stably “+ Mitosis s important in (1) Growth + as talons for an increase in the number of genetically identical cels in a multicelsar organism & contributes to an increase in its Size & mass, (2) Repair as t atows damagedwor-out cals to be replaced (e.g. skin cells) & lost parts of an organism to be replaced (e.. lizards ta) (@) Asexual reproduction > 2s allows forthe production of new individuals from just a single parent (.9. vegetative propagation of onion bulbs) (The fusion of egg & sperm fom two diferent parents is not necessary) where offspring produced are genetically identtcal tothe parents and hence ave akeady adapted to the envionment that alowed the papents to tive ‘This allows for rapid reproduction for colonisation ofthe habitat Rm SEER (0 for maintenance of chromasome number in offspring in every generation + uring reduction division (meiosis), diploid celts (which have 2 complete sts of chromosomes) undergo two nucle divisions (Meiosis | & If to ‘ive rise to haplold gametes (which have only 1 complete set of chromosomes). + During fertiisation, 2 haploid gametes (one male & one female) fuse to gle ie toa diploid zygote. Hence the chromosome number the zygote is restored when fertilisation occurs, + lt meosis didnot occur. the fusion of gametes during sexual reproduction wil resut in the doubling in the numberof chromosomes with each ‘successive generation, ‘+ Honce reduction dvzion(meiosis) ensures thatthe maintenance of chromosome number'n 2 sexialy reproducing species in every ‘generation, (Gi tor maintenance of genetic variation in offspring in every generation *+ During meiosis, Independent assortment of chromosomes and crossing over ensures a wide varity of genetically diferent gamotes are produces + This leads to great variation in offspring produced which result from the random fusion of gametes during sexual reproduction. * During meiosis, (@) Crossing over between non-sister chromatids of homologous chromosomes resus In new combinations of alleles on chromatids. (& eventually a varity of ofspring) (0) Independent assortment of homologous chromosomes at the metaphase plate & their subsequent separation during metaphase | ‘anaphase | respectively & Random orientation of non-identical sister chromatids of each chromosome at the metaphase plate & their subsequent separation ‘during metaphase Il and anaphase I respectively ‘> results in gametes with diferent combinations of maternal & paternal chromosomes, (& eventually ina variety of offspring) “Random fusion of gametes ‘> during sexual reproductionfertiisation resuts in offspring with a variety of genotypes & possibly phenotypes (& hence a variety of ‘fepeing) ‘Frepared by: Mrs. Salvamanl Nair Taos insttoton 0758) meeluiar Functions Gall Nuclear Division 2015-2076 a Motosts Location & ceil | Somat cals im Precursor sex cells ih reproductive organs that ge rise To ‘ype gametes, a No.of nuclear | One (Note: DNA repization oosurs any once) “Two (Note” DNA replication occurs only once) divisions. ProphaseT Prophase No synapsis/ homologues do not pair up: Synapsis occurs homologues pair upto form bivalents(tetrads) ‘No chiasma formation Chiasma formation & 'No crossing over of corresponding segments ofnon-sistor | Crossing over of corresponding segments of non-ister etromatids: ‘@romatids of homologous chromosomes (resus in non Identical sister chromatids win new combinations of alleles) Prophase It Similar to prophase of mitosis Wataphace ‘Metaphase | Chromosomes, each consisting ofa pair of sister chromatids, | Homologous chromosomes align in pairs atthe equator align Individually on equator (1e form 2 single row) (ie. form 2 rows) Each centromere attaches to spindle fibres from both poles. | Centromeres of each chromosome attaches to spindle fibers from afferent poles Metaphase iI similar to metaphase of mitosis excopt that 2 Chromosomes consist of non-identical sisler chromate “Rnaphase | Separation of centromere: ‘anaphase | ‘Separation of identical sister chromatids to opposite poles; | NO separation of centromere; (isthe east | (NB: 1.0nce centromeres separate, each sister cheomatdis "| Separation of homologous chromosomes frequently ‘called a chremosome (Ge. pair of sister chromatids move to same pole, observed phase | 2. Buting anaphase, kinetochore microtubules shorten | anaphase fl astisthe while nor-kinetochore microtubules lengthen as they | similar to anaphase except that non-identical sister shortest phase, slide pass each other, causing the eal te elongate ) chromatids separate Telophase | Zdaughter nuciel which are genetically identical & have the] Talophese | ‘same. chromosome number as parental cells > 2daughter nuclei which are genetically different & each hha half the chromosome numbor as parental cells) Tolophase I > 4 daughter nuclel which are genetically diferent & each _ has half the chromosome number as parental cells) ecu oF ‘Tgenetically Wentical daughter cai fom, “4 genetically diferent daughter cels form: nuclear No variation ocous(n the absence of mutation Gonetc variation has occurred (nthe absence of mutation): division Daughter cels have the same number of chromosomes 3s | Daughter cas with half the chromosome number as parental parental cols > hence caled replicative division ‘els? hence called reductive dvsion a hich can increase the chance cere Pritemrrens on roe pee SEE SEE ‘+ Regulatory checkpoints inthe cell yc that ensue normal call division & growth + Dysreguation ofthe checkpoints inthe cell yele can resut in uncontrolled cel vision * Dysregulation ofthe checkpoins is due to gain-n-uncton mutation in proto-oncogenes and loss-of-function mutations in tumour suppressor Genes. Ths can result in 1) excessive cel growth and polferaion (due to mutations in proto-oncogenes andor tumour suppressor genes) 2 oss of contac inhibition (.e. cals can grow on top of eachother and form a tumour) 3) evasion of apoptosis (Le. cells no langer undergo programmed call death) 4) angiogenesis (e. blood vessels can grow Into the turnout) + Hmetastass (Le. tumour cals may separate from the primary ste and migrate to other pars of the body va the bloodstream and proliferate there) then occurs, the tumour i refered to as being malinnant and cancers said to have oceutted. Gsin-ofunetion mutation > e.g. when a proto-oncogene is mutated to form an oncogene (ominant mutation) > mutation in just one copy of the gene results increased cst {growth and proliferation due tothe increased syathesis/actvty of 2 funcional product (which was not produced previously) due to mutation ‘Thus the mutation Is sai to be dominant. Loss-offunction mutation > e.g. mutation in tumour suppressor genes (ecessive mutations) > mutations in both cops ofthe gene necessary for loss of tumour ‘suppression ‘> even witen one copy s mutated, the nan-mitant copy sil produces @ funcional gene product which will result in tumour suppression. ‘Thus the non-mutant copy wll mask the effect ofthe mutant copy and hence the mutation e said tobe recessive. Metso rect eae erect it, Sven inecergee ts uml cere > egos cavgme a wi wi dnt ncaa onan | MRS eae ‘tonne 9 eprueWcarcses (Yt onan ahi | Shek. erin Beton wn cota ieee. hmepedona a} cea, taro | & Socal yaasan 5 Seana B far nck ct nes apa tots ome ite ‘Prepared by: Mrs. Selvamani Nair Raffes Institution (Wr 5-5) 3Celltar Fanctions s T “ Afior the centromeres divide at anaphase, the ‘umber of chromosomes per cell daubles unt ytokinesis is over. “Since the number of chromosomes halve once the ccall_has_completely divided, the number of chromosomes pec call dropped from 4n to 2n only atthe end of eytokiness. : 5 i z £ i 5 Eel see nes [et |e [enenes fee aree ee |e ‘Sequence of Events ‘During S phase of interphase, DNA repicates and | 50 the amount of DNA increases gradvaly. ~The amount of DNA per col halves when the cell undergoes cytokinesis, 1 > ‘Sequence of Events “The numberof chromosomes por call hale atthe end of | the 1 cytokinesis and haploid cals res. “After the centromeres divide at anaphase Il the number ‘ofchromesomes por call doubles untl 2" C {oytokinesis) is over. ‘Number of chromosomes per cel ‘Amount of ONA per cell (pa) x oy T 5 T oe Pl Mt co Pl oM OATH 2% * After the 1*C (ytokinesis) the amount of ONA per ‘calc rectored tox (came ae the eiginal cel) and the daughter cels ae haploid. : Aner the 2% (cytokinesis), the amount of DNA, Per collis»/2 and the daughter cells are haploid, ee [ee eae |e |e BEE | Sequence of Events AT fc pH om A TH oC ‘Do note that the amount of DNA per nucleus (not shown inthe above graphs) doubles during S phase of interphase. Then, during mitosis it halves at {elophase wen the nuclear envelope reforms. During meiosis, the amount of DNA per nucleus halves during telophase | and halves again ding telophase I Prepared by: Mrs. Selvammani Nair Rafes Institution (56) zDNA repiication, Vanscription, wansiation & mutations 2015-2076 TNE EN (ive carbon) sugar Ribose a Deoxyibost ] Purines (rings) ‘Adenine & Guanine ‘Adenine & Guanine | Byrimidines (1 ing) Cytosine & Ur (Gytosine & Thymine: ‘Complementary base pating occurs between ‘Adenine & Thymine (ZH Bonds) Cytosine & Guanine (3 H bonds) ‘Adenine & Uraci (2H bonds) (Cytosine & Guanine (3 H bonds) Sroctore Single Stranded Double Stranded Found in (oca400) Gyloplasn Nucleus Ntrogenous base: attached to C1 Phosphate group: attached to C5 ‘OH group attached to C2: involved in phosphodiester bond formation If His attached to C2_ > deoxyribose sugar HOH i attaches to C2 > ribose sugar ite. noo purines = no.of pyrimidines * Burnes: 2 ngs (abs er ge gogee AGA) * Pyrmaines: 1 ing (CUT me on arn) * Constant width between sugar phosphate ‘Secor ‘backbone eqpmensyommst | _*2atrands are antrparaet one sand rns Sezer | "inthe 5 to droton, while the other Strand ron the to drecion > BNA ‘pend wohave Grectonalty + Icomplete tan of th double helchas 10 bose ate and span a detanco of 3¢nm a bwAmolecule made up o2 sands of ONA encoun onpesoee a tree g =f z SS how z Sree 88 “Prepared by: Ws Selvamani Nair (@) A stock of parental E coli wore grown for | Shypotheses leation mechanism: ‘many generations in *N medium as the only source of nitrogen unt "N was | 4) i ‘Semi-conservative replication ‘both strands separate by the breaking of hydrogen bonds and each strand acts 9s @ ‘omplate forthe synthesis of a new strand Incerporated into the nrogenous bases of all bacterial DNA. (©) The E-coll containing "N-"N were then ‘transferred into a. medium containing only "N. The transfered Ecol wore Slowed to divide once and wore then Collected. The ONA extracted and egntriuged in CsCl were all hybrid (*N- SN) DNA. This excluded conservative repllcaton in which no hybrids form. (©) Same of hese cals were then alowed to divide once more. The DNA extracted ‘and gentfuged in CsCl were half hybrid (NSN) ONA and at “ight” ("NSN DNA. This excluded dispersive replication inwhich no pure "NN can be obtained ‘Raffles Institution (Yr through complementary base pairing. ‘Thus each DNA molecule formed isa hybrid consisting of 1 original strand and 1 newly synthesized strand. 2) Conservative replication ‘32 parental strands re-associato ater acting as templates, thus restoring the orginal double hel ‘The other DNA molecule consists of 2 newly synthesized strands, 3) Dispersive replication Parental ONA molecule Is fragmented and ‘ispersed, Daughter molecules are madeup of rmidure of old and newly synthesized pars,‘A gene mutation 1 ‘change the 3D shape of the protein, onc Dah & Genomics ~ pu replication, ansernton, ranstation Emutions 20752016 From HbA to HDS. "Two of more nuceotides are inthe wrong sequence | nucleotides are inserted into a sequence Result of mutation Tendon “Tor more codons changed | Shits reading frame fom | Shits reading fame fom point of changes point of mutation mutation Efock on protein —T WinorMajor | Winor Major, depending — | Usualy Major Usually Major fonvwhether a trameshit | H the number f mucleobdes inserted or deleted are a multiple of cours three, there wll change the primary sequence but a frame shift wil ie not result, ‘Examples of diseases due to gone mutation: Name of disease ‘Sicklo-coll anaeria (Cystic Fibrosis Protein affected ‘eta-gobin chain of haemoglobin (Gystc Fibrosis Transmembrane Conductance Regulator (CFTR) ‘Change in mRNA: GAG to GUG Desciption of change | Change in DNA: GTC to GAC (substitution) Change in amino acid: glutamate to valine “Change in DNA: Deletion of 3 nucleotides on exon 10 of chromosome 7 (deletion). ‘Loss of amino acid phony! polar and hydrophobic valine in HPS. together. This polymerization of HbS fect ofthe change | Charged and hydrophilic glutamate changed to noo formation of abnormal, igi, rod-ike fibres, ‘Shape of red blood cell distorted — sickle shaped. Missing or defective CFTR (a channel protein), CF not transported out ofthe epithelial cells of the tissues, ‘At low oxygen concentrations, HBS undergoes an | especialy lungs. ‘conformation change which wil cause the hydrophobic patches on different HBS to stick \Na’ and Cretained within the cells cause the water potential within the call to bocome more negative. resuts inthe | Water retained within epithelial cells esa rest ‘Mucus in the lumen becomes tick and undiuted Bacterial infection may occur ‘fects ofisease | Sickle red blood cells are more fragile ‘energy and heart failure. Sickle re blood cells may also fodge i i “This results in shortage of rod blood cells and poor ‘oxygen transport. Tis loads to anaemia, lack of ‘and break easily. | In the lungs, thick mucus may eause lung infections and ulty in breathing. Inthe pancreas, thick mucus may block the pancreatic duct > Indigestion. inssmall blood | inthe sweat glands wil prevent reabsorption of NaCI resulting in very salty and copious sweat production 30, toeaion cleus (also in mtochondia and ‘crops chlor) [regs at Origin of opication Promoter Star codon AUG) ie geile) Ends at ere 2 acfacentreptestin | Termination sequence Stop codon VAG.UAAUGA) bubs meet Telomeres (Uae we Go vor de a Template RA bom sana ‘DNA feria an cain Sad] [ mRNA Monomers Deonyrbonucieots Ribonuceotdes ‘amino 388 Campiementany —baso- | Adenine & Thyine ‘Adenine & Uracl armpemntary pang bobvean coda ating Cytsine & Guanine “Tymine & Adenine fod antreodon Gysine & Guanine Guanine & Gene Enaymes ioe DNA polymerase, Helicase, | RNA polymerase “inoacyl RNR yeas | Primase, DNA Ligase, TaN Pephentcntrcineinaserrcn) | Paptdyl ransterase (ribozyme) ‘Topoisomerase Bonds within molecule | Phosphodiester bonds, ‘Phosphodiester bonds | ‘Peptide bonds ~ fenmed ees | iysrogen bonds [Ribssomes ivoiverent No ie Yes Tenplae sands eaa'in[ 3105 oeeon 3195 areaion 3 tod diedion Molecule is sytesized in| So 3 drecon ‘tos dvecion ‘tom the amino endo th carton end Prof reading Yes E 3 Produ) DNA TES mRNA RNA NA SSRNA Poypenide chal Product desiiaon Nucleus Gyles Copier Cell manibrane/Ouie Gl ‘Prepared by: rs. Seivamani Nai ‘Raffles Institution (¥+ 58)‘BRA & Genomics ‘BNA Teplcation, transcription, Wanslation & mutations “gorea76 The main role of DNA is to store information and pass it on from one generation to the next, Its a suitable store of information a: 2) ean be replicated accurately > daughter cells have identical copies of DNA as the parent call ‘Weak hydrogen bonding between the two strands alow them to separate and act as a template for new strand synthesis (Adenine forms 2 hydrogen bonds with thymine and cytosine forms 3 hydrogen bonds with quanine through complementary base paiing) by Iie a stable molecule > can be passad onto the next generation without loss of the coded information (Why DNA needs tobe stable?) Coectively, numerous hydrogen bonds hold the two strands of DNA together and adjacent nucleotides In each strand are joined by strong covalent | phosphodiester bonds There isa backup of code [DNA le double stranded and one strand to serve as a template forthe repair ofthe other a mutation occurred 4) Coded information can be readily utllsed/accessed Weak hydrogen bonding allows the template strand to separate from the non-template strand allowing transcription to take place ‘Complomentary base paifng allows the fatful transfer of info from DNA to RNA in transcription, which wil be translated to protein subsequently EES My Messenner RNA (mRNA) serves 25 a messenger that, n eukaryotes, takes the Information out ofthe nucleus via the nuctear pore to the ‘cytoplasm where translation takes place. 2) mRNA acs as a template for translation, as each codon witin the coding region ofthe mRNA represents an amino acid in a polypeptide. EE Mrhey bring in specific amino acids ina sequence corresponding to the sequence of codon in mRNA tothe growing polypeptice ‘ean facitate translation due to {hits ably to bind to a specific single amino acid {ete abity of te anticodon to base-pair withthe mRNA codon SEO (CD FRNA associates with a set of proteins to form ribosomes. {@) FRNA isthe main constituent of the interface between the largo and emall subunits ofthe ribosome ‘Thus the small ribosomal subunit can Bind to the mRNA 3s complementary base pairing can oocur between the rRNA in the mRNA binding site ‘of the small ribosomal subunit and the mRNA. {@) FRNA is the main constituent of the P ste (peptidyHIRNA binding site) and A site (emino-acy! tRNA binding site) on the large ribosomal subunit Hence rRNA enables the binding of aminoacyl-tRNAS to the P site and A site (4)An RNA molecule (peptiy| transferase) on the large ribosomal subunit also catalyses the formation of the poptide bond between the amino group ‘ofthe new amino acid in the Ase and the carboxyl end of the crowing polypeptide in the P sit ‘Prepared by: Wa, Selvarani Nae Rates sttaon OE] 7DNA & Genomics PRINS ON DNA replication BOI 20. 4. Before DNA replication, free deoxybonucleoside itiphosphates are manufactured in the cytoplasm and ‘ansported into the nucleoplasm via nuclear pores. 2. NA replication oocurs at § phase of interphase. UNZIPPING OF PAR! '3. Replication begins at specie points of the ONA molecule ‘each of which fs known as an origin of replication (or). 4, Hellease binds to origin of replication, It disrupts: hydrogen bonds between complementary base pais, ‘using parental strands to unzip and separate. 6. Single-strand binding proteins keep the strands apart so that thay can serve as templates for the synthesis of new strands 6. Topoisomerase relieves “overwinding” strain ahead of replication forks by breaking, swiveling and rejoining DNA strands. [ADDITION OFPRIVER 7. RNA primer is added to each template (parental) strand by the enzyme primase. 8. RNA primer provides a free 3 OH end for DNA polymerase to recognise and start DNA synthesis ofthe ‘complementary daughter strand. 8, ONA polymerase ean only add deoxyribonucteotides (ONA ‘nucleotdes) to & pre-existing YOH end of 2 rucleotide. 40. DNA polymerase uses the parental strand as a template ‘and. signs the free. activated deoxyribonucleoside ‘triphosphates (QNTPe) in a sequence complementary to that of the parental strand. 41, Adenine base pais with Thymine and vie versa ‘Guanine base pairs with Cytosine and vice versa. 42. DNA’ polymerase catalyses the formation of phosphodiester bonds between adjacent daughter NA /ucleotides of the newly synthesised strand, 43, Removal of the pyrophosphate (PP) from the deortivenucleeside Uiphosphate (ANP) and the Subsequent hyorelyeis of PP: provides the energy to drive the polymerization reaction. 14, As DNA polymerase moves along the template, it proof reads the previous region for proper base paiing, Any incorrect deoxyribonuclootide is removed and replaced by the comect one. 15. The leading strand is synthesized continuously jn the 5° to’ direction. 416, The lagging strand is sythesized discontinuously. Its synthesis Is similar to leading strand, except that the Tagging strand is synthesised in fragments known as ‘Okazaki fragments. Each fragment is inated by an RNA primer before the addition of DNA nucleotises. 47. different’ DNA polymerase then excises the RNA primer and replaces & with decxyabonuclestides. 18, BNA ligase seals the nicks by forming phosphodiester ‘bonds between adjacent nucleotides of the each of the [ONA fragments on the new strand seas 49. Complementary parental and daughter strands rewind into ‘a double helix. 20. Each resultant helix consists of one parental strand and fone daughter strand. Hence ths is called semi- ‘conservative DNA replication. ‘origin of replication (or) a eS hatcase IS rand binding proteins replication bubble fe RNA primers are added by primase Send of RNA, primer DNA polymerase eoxytibonuclooside trghosphate/ DNA nucleotide complementary base paling & : ‘Together tho Okazaki fragments form the lagging strand Tn aM a a diferent DNA polymerase replaces the RNA nucleotides with DNA nucleotides DNA ligase seas the nicks by forming @ phosptodester bond baween adjacent fuclotides ofthe 2DNA fragments of | _the new strand nT | Prepared by: Mrs Selvamani Nair Fates Ttaton (5) 7z GW) wanna soypeH Tien WrewieNOS San RG peveC aI 6x0 ou seu PuE ve vs “ 281 PUB ua 1uwop tepuoeienu euuape sppe WoIuN ases0Uuhod vy Ajod awhzue eu) hq (uoHelKuapediod) 1) ¥y Ald Jo stsaunuhs “¢ 8 Gulpoo}euoxs uf» "bes Gulpoo-Lou)suosyu esfoxe YOM sewososcyds AG (dy Sesnbe: Youn) Bulsnds YNZ 7 Uo} YN aimeuyo yews bjs uojuBooes © P wos ‘enwajai 640) eveiaunkod ‘yn pue yay uy sosneo veut wna "yNaureid 9 ul (vwwnyy) eusIs uoRerAuepesod © 20; s9p09 Yow 'YNG 8yp Uo eouanbas @ saquosue.n asEzOUuAOd YIN | NOUWNINESL NOUWNINEAL ‘SSLOABVHOWG NI ‘SELOAMWINA NI ‘vu doo} uiduyey dunsuea vat ‘sleouuees ‘poquiosuen we0q snf sey yup YN Jo Uo|S=1 Uy "VNU BurzsaKnUKs pue ‘spuens z aug Bucehzun “jay anop YN 84) Wop enow Cl sanunucD xejduioD LoNduOSUBH Bui SY “9 ‘uonDeup.s 0} ¢ 94) ul Pea! 8] puEN|S YNG seIduIE ax) y UONDeNP ¢ 01 § OUR UI pereBUOIO W Poziso\aUAS 8] PUB: 1 pUELIS YN Bumcu6 ou) J PUD OU 3 Den NEU ou snuL'S sdnos8 ayeudsoue jeutauo} udsou janurogu W029 Sy “> seeseuKod YN ‘9869 ouluh 12d 0569 0 ‘Aiewuowoiduion Aq pues YNG SreIdUe} aun Yim dn yore sepHoBionuogN 32. NOUWONOTS SELOAUWIOUG GNY SBLORUVANS NT “YN as eoKRUKs oF (puene Sujpoo-uou ow ose s| pueas eveiduiay Sus GN) ‘se poen et pu Uuesnjoq epuog ueBouphy ‘Supa Aq otowe1s uote ojquiesse yuy s10120j uondssuen jes0Ue5 Z anna op apelngy e' SeeDOUAA YN NOUVULINI SSLORAMONA NI oN vob oo suevodues yew e Taran en2a0) coteemnay anoweenn ad exer via Ben Ye NOTES OR SHOE wonaasueL 'S2]WOU0D % VNC.DNA E Genomics Translation 2015-2076, ETNTMAIIOIN tre synthesis ofa polzeptde using genetic Informalion encoded in an mRNA molecule. There is @ change in Tanguage” from nucleotides to amino acids aminoacyl RNA lently attached tothe 3' CCA stem ofa specific tRNA by a specifc eminoscyltRNA synthetase. 1086y! {RNA synthetases. Each enzyme recognizes a specific amino acd & the unique ientty sites at /YRINAS can be formed, IATION th EUKARYOTES & PROKARYOTES) (if eaves) INEUKARYOTES: “= Initlation factors and ‘RNA associates with the stat codon by complementary base paring jowed by points 2-8 under ination.) ELONGATION a= {nboth UCARYOTES & PROKARYOTES) iis euros) i 1. Codon recognition * Antcadon of ncoming eminoacyl tRNA base pairs ‘wth complementary mRNA codon in A site by forming hyerogen bonds «The process is repeated ur 8 stop codon is reached. TERMINATION Tnboth EUKARYOTES & PROKARYOTES) (fis (UXGA oe uaa) n of proteins) and prokaryotes. rapared by: Wis Seivamanl Nair € Ms Emaline Choo aaffes Institution, Viruses {ses ate Considered iving ornomiving? Living a they contain genetic material. However, non-living because they have No sganization and only show characte ings Include1) metabolic activity 2) cellular organization 2) abil reproduce and grow in numbers. ond to stimull and adept to environment ate parasites? This is bocause viruses, lke obligate parastes, depend on host cells to complete the lite cycle. 1 Bacteriophages: ‘Animal Viruses. Sze: 10-300nm ee Envelopes Ta] tambda | Tafenea Fluman fmunodatieieney Virus phage | phage + Docbie- 7 = 3 codes for synthesis of viral components and ‘stranded DNA tary to viral mRNA ‘plication & assembly + Laifferent segments of single stranded RNA associsted with | jouble-stranded ‘hucleoproteins Each RNA segment is packed with 3 polymerase protelns together to form an RNA-dependent RNA ‘Simplex which replicates anc transcrves host col + Teosahodral [= + Protein coat that surrounds atid protects viral genome capsid head + Comprise subunts called capsomeres Envelope, + Resent 7 Giycoprotains embedded i envelope: Rasmaggitinin (60%) & |» Glycoprotein embedded in +" Phospholipid bilayer surrounding the nucleocapsid ‘neuraminidase (20%) pe: opt . ‘rom bos is altached to gp4t Embedded with al glycopr 2 copies of single Roverse transcriptase Bg Hsemagalutnin Neuraminidsse Envelope ot ‘Tal surrounded by contractile. —| sheath capsid RNA segments, Base plats integrase 2) nucteoproteins Envelope Capsid Tallin ‘9p120 4 phage Lambda phage Influenza Virus Human immunodeficiency Virus Mons requenty occur due o he poor proofreading mechanism ofthe viral RNA-dependent DNA polymerase. Over these mutations produce viruses with modified (eg siycoproeins euch as haemagglutinin or neuraminidase) these modified antigens, the host becomes susceptbleto infect a host that does not ral of intuenza A and human strain of influenza A infect sing fembled in the host cel, they can have new combinations of RNA segments, Sometimes these viruses infact a human host thal does net have the antibocis thal recognise these modfied antigens, the h reassortment can occur. Thus when new ‘lvcoproteins such as haemag he viv. Prepared by: Mrs Selvamani Nair, Mam Sharon Cross and Mrs Wong Seok Hulz coe co {ni x00s 6uoy s1y pue ss049 uaseus WP “EN jMeweAres Su :Aqpezedeis ouuoy AMsu Oi) eseoye: pue Sash ouE:GuISW}eD eUEDEE + . oseaieu'y suyojesdoo4i6 jeu s10yr ouesquiew! eins ‘YN 2U WII ie|2088e sujsiosdo;ONN + | sos Je sojquiasse UlsjoudAod pue wou auesu| sierduico are sujioidoof6 jenn soy aves 8 u lol» Ayuopusdopu porquesse si0ay ‘peoy «| joAquessy | eo Wo Wn eeposse svotald plsdeg + | PERU pallj-YNG # Ol] equesse psc 2] “Monesmew e | “Tyet woYeITE9 TaN BIS ‘oni jo aeeud uojeaidos pospx uoyls| aBeudodd au» sugioid sozvaded a Kanes AL, seus oxjeoututs 01 osn | Aiouruoew Burieaugute eoysoy ow | pisdeaoojonu € euesqwew yoo 1804 (eusiquiew jo uojeujbeAty senonu| ss000%0 AUS PAIN 3UN "L¥dB Jo dou ou WAN» | __ OU) STECUROOPUS Ag yoo Sou seu STA» 16s06 jo sou ol] PEGEOIO SeEaIE | -00 240 day ovp wi (sabeudosoew) 0 04 UO 304 Luo sieide2es pap kreiuowaidwo> ot «| onwousiéivos or sous uupnsBewen + i190 ou Uo seynoayoUl oyde0e% ayeoeds 01 pug o susie.dooK|B eA 96n sesrn pOdOIORUS sin wouyseny' sobs KSA 7 : Fo TORTS Fae SInSSIOE2015-2016 Raffles Institution, Viruses () New formed viruses bud off by evagination, membrane with emibedde acid receptoron oe host membrane. (hich involves Invagination of membrane) “ae Te lymphocytes (or macrophages) with th (3a) Reverse transcriptase ‘makes DNA strand using via RNA as template > RNA (4) Nucleoproteins degraded > 2" DNA strand ‘atsoclate with the RNA genome and then A ntearase integrates ) J oNAT ia ‘embedded on the plasma membrane. This ntiates the budding \ atycoproteins fowased into cytosol 2) J Ouys0s0me —— oa a \ cS — = RNA o Yon! ae \ en sete cupmnnncnyed | Soencnone sai me mnie gal Reet mae at oF wo NA areshown Phan (99120 and gp 41 in the RER which cevertualy are embedded Inthe host cel surface neighbouring cals. Ty of influoraa, Pathogereeity FHV, Tare 1 n infivenza wil bind to sale acid receptors on epi ‘respiratory tack han HIV binds To COM Teceptoron i Trl ape oT WE 1 v Infuerzarapicates vii and then bus of nected i eventually se HIV replicates within It and then buds ra cted T helper cels eventually lyse. ‘The build up of dead epithelial cols resis In infammation and symptoms of nfuenza appear | With fewer T helper col, the immune system is seprested 8 ind more susceptibie to ‘Sunny nase & seratchy th ‘opportunistic infections. When infections become unmanageable-PAIDS > death high rate during repication Prepared by: Mrs Selvamant Nair, Mdm Sharon Cross and lirs Wong Seok HulnH yous Buoy s1y pue ss019 voreys WpH ‘EN [weWeni0s S11 :kq pEzedeicy Tengu] Wo) eB eeTOTUB] J6 BAT OA reese supeyaid pus owoues ee) Ayquseey @ sued L518 POH, ~t 4 + NON St @ NOS vamaninae Ss. Md HAT 10 919K OT ~ = ud Soman Senet