Monosscchares Features — =P op pol oraIa CRO P Fence [2 Rea cortony (O=0) acum SAN YP | 5 spate ne nave muse hydrony (OH ups NA a Some H bond wih water nd hones en Solbl in water an oasy anspor in sna and aye NOY ton rrp sysone ~ oe “tings extend tse (2 iOH gp at ts lw ng and on pone ie of 5 aghcose — ohcose tnd BOM grpatct i sbovering ad on same sto C8) (ote mat on now ore can | 8. ot redecing sugar overs mores). 25 ghee, gscore sd tucose | Diacchardes Features 7 - ae {Se made up of WONOSSGNAGE i By 3 GHVEORETE Don Toone DANG Wo HONORE Zz es ij condenanonroncton ft toes te os of a wetor elec A\y yi Ny | 2, Gnvountine nereompenon montsaccaes ee hart reaction ware, whe ation au oh. Koy ‘Stone alco of water, te pcos bond con bo oxen 1 oa |», many yon arupe externa a ote z vo “Se tes th water ance rosy soluble i water ns easy tanspotedn animal and ogicosr est, couove antarapot eye general ome 2. remade up of many monosaccharides joined by alycosic bonds formed between them by | ® condensation reactions wiuch woe he ls of water molculs. Pomnt of Conpareon Sure __Giyeogen Calllos Funcion | Plant torage poyeaccnanda —| neat atorage plysasmre —| Plat structural paysacchare [Lacston Stored as granuls n eloropiais ‘Stored iver nd muscle cals | Coll walls of plat cals Monomer “Tide up of glucose monomers | Wade up ofa-glucose monomers | Made up of Plucose ronan Bond batwean | In amylose: a(t) gheosise Bond Enis | o(t4) glycosiaie. bond inka |B (4) alycossic bond Wis | ‘monomers monomers ‘monomers witin a brench and | Monomers ia molecule In amylopectin: (1-4) glycosidic bond inks | a(t) glycoside bonds ins monomers win a” branch end. a(-6) | ronomes branch ports fyeosidie Bonde Frks monomare at banc fons ‘Gierlalon oF [Al gcse ans he chan have he same | A gloss unis the chai have ‘monomer extention the same onentation ‘Studure of each | Amjiose a alia —maieaua wile | Helical and. branched molecule, | Long, straightinearehsin rmolecale “amyopoctn’ a helical ‘snd branched | tke amylopacin, bul more mace ‘extensively branched ‘ans between | No aera yon Boning Wo inierchah hjergen banding [OW groupe pojecing ouwards ae botn “arectone allow "sterchain drogen bonding = eages mirofee ocmation low the siructares of starch and alyeogen mak tiem good How he aractare of calaze nates ra good ‘STORAGE molecules ‘STRUCTURAL moecute “large maecule made up of many e-glvcose mosomers "Adjacent glucose units are inverted 100 with respect io each other Hence I huge energy store se can be hyertyed to yielé | ana hence fom a near molecule wi fee OM groups projecting ot in both trary glucose molsaies tha can be used ae 2 respiratory | dtechors wich can hydrogen bond with OM groups of other callulose ‘subetrat to obtain ATP. ‘molecules lying paale tt 0 for macrofbris Thus he mcrotonis have high tonsil strength. 2. Compre of alias ‘3 can pack many subunits per unit volume 2.Asa macromoloce, coluose has few OH groups available to hydrogen Bim which most OF groupe ae mvoWed Io Intramolecular H | bond with water as most are vlved in inerchan hyogan bending. Th, ‘bonding. fow OH groups avaliable for H Bonding wth water. | ony We srtaoe of tuo rot has OM groupe that ean Nysrogen bond Fence tay ate insoluble In water and the Ww of cae ae | wi water. Thus callloce fs insluble Im water and the Ww of cals are ‘nafected by thei presence Unatoctod byt presen, {3. Amyopoctn ae gycogen are branched 3-The mother of mics that for the oot wall havea porous structre ‘2 they have multiple Branch ands which hyoic enzymes can | and ence makes thecal wal work on Thus moe gucose molacules can be relatead and | &reely permeable 10 walor ond sais and allows movement of ‘more. ATP can be gonerated by respiration por uni time. Sitctantes in and out of cls branching optimizes packing of any subante per unt value | —b. strong ac ngid and prevent he pant cals fom bursting due to csc Sand hence more energy can be stor por unt volume, ‘sess branching reduces the sceessibiy”of wats and thus ‘educes the solubility of tho molecule, Thu tho Ww! of cae | 4, Colutases that hycrysecallose are found in very few organisms. Thus ‘re unaiacted by ter resonee cellulose cannot be hydrolysed and used as a respiratory substrate and is ‘Sigood sigur mato Frapred bys § Nat & ws Wang SH aes ttn (59) za 0 a Benediets Yost | 1. Place of eat eakaon ina Wat Ue, {orReducing | 2. Aad equal volume of Genedits eegent Sagare 3. Shake te mtr, ‘colour of Soa sluton depends on amount of reducing sugar ‘© Heat by ieersiog the tute in bling wate bath or | present ete sem-quanttye) Strict, ‘Svs fom green yao ie boin to rick ed “Tei Tor Won- | a nagalive veal or Banedict= Wat SHARE Tor te | Presence of non weaucing aparece | Reducing test son then Sugars bow equal volume. of test solon with ute hyoerione sek for out 1 mite to Myers Amino Acids ~ Baie structural unt of protoine "Structure © consists ofan edrbon atom covalently bonded to 4 groups ‘hydrogen atom, 2) amino group (NH), 3) carboxy group (COOH), 4) variable R group + Properties of amine aclas (© Classified according other R groups 2s pola, charged or non-polar © Exéstas zwterons in seluton = cary both postive and negative charges, © Actas butters > “Can donate or accept Ht, therefore able to act as an acid or asa base — amphoteric > Essential in biological systms ~ sudden change n pH could adversely atl perfomance of protein tke enzymes + Polypeptides "Amin acs ae joined by a peptide bond via 2 condonsation reaction wth the removal of one water molecule + Further addon of amino acids resus in the formation of tnear polymer called a polypeptide ‘© Reguary repeating par, the main caine refered to asthe backbone, © Variable part comprises te disnctve variable R groups “+ polypoptide folds inte a spect twee-dimensional shape / conformation ‘+The nucleotide sequence in DNA determines aa sequence in polypeptide which detemines types and locations of R groups which detemnines group interactions which determines 30 structure and function of protein. roy + levels of oganizaton athe acre otra ‘+ Refersto the number and sequence of amino acids i Linear structure maintained by peptide bonds *+ The sequence of amino acids and thai R. groups) i a polpentie chain determines the ‘ype and iocation of chemical bonds/interactions, and hence the 3D conformation aid * | characteristic ofa parteusr poten. * Refers to the spatial arangement formed by regular collag or pleating ofa single polypeptide chain in one direction. ‘+ Maintained by hydrogen bonds at reguarntenats © Formed between CxO and N+ groups ofthe polypeptide backbone, groupe are not involved Made up ofa single polypeptide chan which ie wound int a colled/splrat stu. ‘A hydrogen bond foms between the C=O group of one amino acid residue andthe [Ne group of another amino acid residue four amino acide away along the backbone ofa single polypeptide ‘There are 3.6 sino acid rosidves in every tur ofthe heli © Beleated shoot +7" Two oF more regionsisegment of a single polypeptide chain lying sde by sido are ‘inked together by hydrogen bonds ‘+ Aliydrogen bond forms betwaen the C=O group ofan amino acid resiue on ‘one segment and aN-H group of another amino aid residue on an adjacent ‘Segment along the backbone ofa single polypeptide + Chains may run parallel same crecon) or ant-parallel (oppose directions) «Forms flat sheet weich becomes folded ‘+ Structure formed by further extnsive folding and bending ofa single polypeptide chain, ghvng ise to the specie 3D conformation ofa protin ‘+ Maintained by a types of nerstions _ © hydrogen bonds, ionic bonds, hydrophobic interactions and disulfide bonds: | ge atc os ane ac ike ‘+ Refers o the association of two or more polypeptide chains into one functional . protein molecule Hise + Mainsine by al 4 types of teractions oe © hydrogen bonds, fonic bonds, hydrophobic interactions and dsutide bonds Bstween 29 formed between R groups of amino ack resitues of diferent polypenties + Constituent chains of a mutimerc poten canbe iencal or diferent Othe: ‘Prepared by: Wrs'S Nair & Mra Weng SH Rails stitution (VF 56) 7Funeton 2 Each subunt fs aranged so that mest of ts hydrophilic ‘amino acd side chains are on extemal surface whe ts & nova hevsens | hydrophobic amine acd sidechains are bured in interior Biter asthe | 3. The 4 subunits held together by intemolcular interactions Saeed formed between R groups (hydrogen bonds, ionic bonds an hhyophobiciteractons) No dsubhide badges, s Haomogiobin "| 1. Hacmogibin has a quaternary sinduie mad up of 4| dre" of haem Group binds temporanly to Oyo 7 HS (Globular roti) | "polypeptide subunits: 2 globin sibunts and 2 Bolo | molecule can carly up to’ Or at & tive loony Stranspors ‘subunits, Each subunt fs made of globin palypoptige and-a | _aryhaemeglobin ygeninthe prosthetic (non-protein) component called haem group. Each loos haem group consists of a porphyrin ring and an Iron ion Rim, toare | (eee red ‘> Thus haemoglobin is soluble in an aqueous environment. can be transported and cary fem hinge totssuee vies vera PAs 2 resut binding of one oxygen molecule to one ‘haemoglobin subunit induces change ‘remaining 3 subunits so that Wei affinity for onygon Increases. Tiss known as te “cooperative binding of ‘The tropocalagen molacule can form a compact coll 3s. almest every third amino’ acid in each Polypeptide cain is a glycine, the smallest “amino acid. This allows ito Ht mio the rested ‘space inthe canter ofthe trp he, f 9. Extensive hydrogen bonds form between ‘esidues of the polypeptides, hence interaction Ww wator moeesies ae hited, ‘ 4. Adjacent topocotagen molecules ae aranged in} ‘a staggered manner 5. Crosssinking "(iwoWing covalent bonds involving Wysing residues) of adjacent {ropocollagen molecules resus inthe fomation of ‘ris. 6. Bundles of fos together form tage and tong SY collagen fea, Bea o.saca a oxygen, ‘Catagen TA collagen molecule (aka tropacollagon molecule) congis (Gbrous prosin) | of three helical polypeptide chains {not o*elces) wound > ancesental ‘around eachother tke rope (is quatemary structure) comgonentof | | 2. Each chain conlins about 1000 amino acs and contain a | ->Bulky and atively ilexible proline and hytroxproine connective tssve | repeating sequence, usually a repeating tipeptise unit | residves confer igety on tre pecea Inthe human glycine, where’ X'is Usually proline, Yi usually body. hhydroxyproine. ‘Piereases tensile strongth (abit to resi snapping due to setching) and increases tensile strength and makes the molecule insoluble in water ‘>Steggeredioveriapping arrangement minimizes points ‘of woaknesses along fas "> Greatly increases tonsie strength. ‘Parge size of collagen makes 2 insoluble, an impontant Property fora structural molecule Fibrous prota ‘Globular prota Mie up of 10s large an mtod ns ably Yo form hydrogen bonds with ido chains forming res Made up of poppe chain folded int roughiy spherical shape. Polar R groups are exposed to water moleciies in te aqueets | water insoluble in water since extonsive hydrogen bonds already formed betwoon residues indent poyperides, cevionment> Soluble In water since these par groups ea form hhydrogen bonds with water molecules, ‘Less variety of amino acid are used to construct he protein te. consists of repetive regular sequence of amine acts. (en ‘More variety of amino acids aroused to coatnudt the preva ie. consists of nonepetive amina aid sequence tripeptide, gy-X-¥ repeats n colagen) Length of polypeptide may vary slighty betwoon two Samples ofthe same protein, yet protein ssl funciona Length of polypeptide s always Kntical basen to samples of the same potin,o eles protein may not be funciona. colagen aemogobi Test Procedure “Observations and Deduetion ——| Biuret Test [1 Place 2anoflest sokaion Wa est hube Presence of proton indicated by 8 2 Add equal volume 05% NaOH solaion ‘purple colour developing sow. (A test for | 3. Shake the miture wot | Beptide bonds) | 4, ‘Add two crops of 1% copper sughate soln, shaking well after each drop. Denataraion of protoing: of {a) Heat (afec hyarogen bonds, hyarophabic interactions) (©) Accs!Akals afect hyéropen andionic bonds) {6) Inorganic ions (tect orc bonds) (@) Organic sovents (atfect hydrophobic interactions) (@) Mechanical forces (fect hydrogen bonds) NBi_1. Pepi bonds not alfected. 2, Stenghh of bonds: hydrophobic intractioncH bondscionic bonds disulphide bridges Enzymes are biological catalyst ~ they speed up th fate of reaclions and are chemical unaired ai ha end oT he reacion & thus ean Be eused, land are efecive in emal amounts + Most enzymes are globular proteins, each wth an active ste with specific 3D conformation that is complementary in shape and charge to 3 spectic substrate + The globular stucture of enzymes contribute towards thir solubilty + Tmadeis explain why enzyines are highly specific: 1. Lock & key hypothesis the enayne’ te lock) acve ste has a conformation which is ‘Complementary in shape and charge toa speciic substrate the key) ~ Slowing the substrate to bind, hence forming an enzyme-substrate complex > products formed no longer ft he active ste and wif hence eave the actve ‘he, making avalable for ancthor substrate to bind 2 Induced ft hypothesis ‘Sinding ofthe substrate to the enzyme active sie induces a conformational ‘change Inthe active site ofthe enzyme such that now provides a more precise ft forthe substrate thus enzyme ean perform ts catalvi function more effectively 7 Taian enayene-celaiysed reactor: 3" Effective calisions take place between the enzyme and substrate 3 _ Resulting inthe formation f an enzyme-substrate complex. 7 Armin acids residues that make up the enzyme have diferent fancions 4"Contact residues ~ found inthe ative sito hop fo postion the substrate inthe correct orientation via weak interactions such as hydrogen bonds, ionic bonds & hydrophoble Interactions. 2. Catalytic residues found inthe active site ~ act on bonds inthe substrate and help to catalyse the conversion of substrate to product 4 Structural esigues interact with each ater to maintain he overall 30 conformation ofthe protein 4, Non-eseartit residues —Tound on surface of he pretain = no specie uncon > Enaymes speed up metabole reaclona/alowa metabolic readions to proosed at moderate temperatures by lowering activation energy (Ex) of to reaction, through: Stee [seer 1. proximity effects temporary binding of substrates in close proximity nthe ‘enzyme active ste increases chances of a reaction (vs ‘Sepending only on random collsions between reactant the abenen of enzymes) 2. strain effects ~ slight distortion of substrates as they bind to enzyme ‘strains bonds in substrates that need fo be broken for reduets to form 3. orientation effects — substrates are held by enzymes in thee active sites in an the ‘correct orientation such’ that the bonds. In substrates willbe exposed to chemical attack 4 microenvironment effects enzymes ereate the appropriate Imicroenvironment fora reaction to ocr e. hyerophoble amino acl in enzymes create wateree zone tha alows non pola reactants to react more easily 5. acid-base catalysis — groups of acidic and basic amino acids in enayme ‘delve Ste facltate reaction between substrates Hence there wil be a greater proportion of substrate molecules with energy sreater than the activation energy, allowing the reaction to procood faster than Suscatalysed reaction = » _ > Erayme cofactors 1. Jnorganie Ions (eg. magnesium ions in PCR) “3 mould enzyme or substrate and alows enzyme-subatrate complex to fom more easly 2. prosthetic group (e 9. haem group of cytochrome oxidase in eocron transport chaln in mer mitochondrial membrane acoeptseletons from loctrome C and transfers them fo oxygen to form wate) > permanenty bound to enzyme 5 ranstors atomsfenemical groups between active ste of enzyme and another substance 3. coenzymes (e.g, NAD transfers elections in certain redax reaction in respiration) ‘5 are organic molecules that aro required by cotain enaymes to cary out catalysis 3 they bind to the active ste ofthe enzyme and paripate in catalysis but ae not considered substrates ofthe reaction 5 foncion as intermediate carers of electrons or spect atoms that are transferred in the overall action Prepared by: Mrs § Nair & tire Wee SH ‘aftes institution (Yr 6) 1Misring ale of produ formation Mess rate 6 appearance of abate 2H0:——> 2140 +0, cataase Starch > Rosucing sugars aie Soe Example 1) Bue ancknpesenceaadne > incompaedigesion ot tach 2brownin presence oiodne "> compte peat sas tains" _| Vane ot Os eves pe nttine ora fader ot tine | Change in etny Bue ack cation compan : gorun tne ova feed pte tne Feed | SERGE aE ae ene ECO Concenvaton af subst ders Ta la arate | Alte contra iat afer oneneymecaayod easton, | Alar cons het ase oe sakes raion eo a 29. pH, temperature kept constant temperature kept constant Sapa z : ——— ot Dropper n LOCO iene 000 — woe 00004 Mite Note: Deter tte may be tced ect tapas ing. 1. Aad enzyme (amyase tsar and sla te stopwatch temas 1. A enaye (alae) to HO, mi and a the 2. Aided tne tera, ante 3 dopo the reaction mire Sopa, ‘Sewntetie wi aay fans procetu | 2 Or craved canbe meas by te dowd 3. Inne presence of alae tans om yeloweh own o Sipcenertt water godt ejnde fs shown | > sure above) orang aeons es oy 4 Ines of ue lack cluraon an be measured using 3 3. Rec vlime oO; eve ot ae vente corner 5, Ula tundard ceo comer the eee edn to starch concenaton Gran fate Ina te of econ = Grade ofc at tne Oe Inna of beak cloaton cencentaton of starch decreases en __| Volmo sf, eed increases wi tine wanes Rate of O; production decreases wit) tme Rate of change in intensity of ive black coloration / Rete of decrease of starch decreates wih ne + Toinvestgate how factors tke pH, temperature, fenzyme o [substrate] can affect the rate of reaction: © Vary independent variables e.g. pH temperature enzyme] [substrate] © Keop all ether variables constant ‘© For each condtoa, plot a graph of amount of product formed vs time and obtain the iil ate ofeacon © Plot graph of rate of reaction vs the facor investigated (pi! femperatue I [enzyme aust) Wales Prepared by: Mrs 5 Nair & Mir Woe SH Tats intttion (¥r56)AT ‘As temperature increases, Sic of enzyme and substrate molecules increases Frequency of effective collisions betwoen enzyme and substrate molecules increasesses Srrate of enzyme-substrate complex formation increases Number of substrate molecules wih suficient energy to overcome the activation energy barrier and {orm products increases and rate of reaction increases Temperature coofficint, hs = Rate of reaction at (x+10)"C ‘Rate of reaction at x°C ‘When Qw=2, fr every 10°C rie in temperature, the rate of reaction product formation doubles. Beyond the optimum temperature, KE. of enzyme and substrate molecules continue to increases 3 intramolecular vibrations increases hydrogen bonds, sone bonds and hydrophobic interactions that maintain the 3D conformation of tho zyme ae disrupted (C Covalent leiphide bonds are harder to break and thus can withstand higher temperature. Hence enzymes with higher optimum temperature tend to have aarger proportion of disulfide bridges. ‘or more itramelocular interactions) 2 Speci contrmation of active sti lost 3 Substrate no longer complementary to the shape and charge of active sit and cannot bind tot | 5 Rate of onzyme-substrate complex formation decreases and rat of reacion decreases. 201526 tect of ot ‘At optimum pl, +S Conformation of enzyme active ste fs most deal for substrate binding and rate of reaction is highest [As pH deviates from the optimum, ‘ Ercess Hor OF tons affect the lonisation of the R-groups of the amino acids residues disrupted > Thus the interaction betwoen substrate and catalytic residues inthe active ste of enzyme is disrupted 3 ate ofenzyme-substrate complex formation decreases 3 Rate of reacton/productfomaton decreases (Note: ifthe change in pH aflecs te charges ofthe groups ofthe (Q) catalytic resiaues inthe active ste, the catalyle activity of enayme may be fst (2) contact residues in the ace sie, this may affet the temporary Binding tween the fenzyine and substrate and thus no enzyme-subctrao complex ome @) Structural residues, the trtiary structure ofthe protein and fs active site ean be affected and this woul denature the enzyme, ato of reaction ‘optimum pl cosrumpet o18yPe of pepsin Effect offenzyme] Init, when enzyme] is low, a5 fonzyme] increases, 3 Frequency of effective colisions between enzyme and substrate molecules increases. > Rate of enzyme-substrate complex formation Increases and rat of reaction increases Ainear portion of graph, enzyme] is timiting Increasing [enzyme] wil result in a proportional increase in the rate of action [At curved potion of graph enzyme] snot the only ling factor. Same other factor als iting ‘Atte plateau, [enzyme] is no longer the limiting factor (Other factors are liming) Iereasng [onzyre] wil not affect the rate of reaction fect offsubstrate] Int, when {substrate is low, as [substrate] increases, > Frequency of effective collisions between enzyme and substrate molecules ncreases Rate of enzyme-substrate complex formation increases and rate of reaction increases as active sites ‘of enzymes are readily available and substrate concentration is limiting Beyond a certain eubstrae Al acive ses of enzymes are saturated with substrate at any one point in ime > feubstrate is no longer timiting and enzyme concentration is imitng, the rat of reaction wil remain ‘constanigraph plateavs) and reaches maximum velocty(Vau). Michaelis constant im: [substae] at which reaction proceeds at half ts max. ale > Low Kin high afinty botwoon enzyme & substrate > High Ke — low afinly between enzyme & substrate Rate of reaction Maximum velocity {Micnaae constant ‘Subauate conceraton Prepared by: Mrs 5 Nair & Mrs Wee SH ‘Rates Institution (¥F58)Cellar Fanetons Enzymes 20752076 ‘Competilve inhibition Non-competive Inhibition. ‘Allosteric Inhibition Activation. Tahir /Raiator binds ‘Active site ‘Site other than active site loser site Shape and charge of inhiitor 7 Siniar in conformation and change | Not senar in conformation and | Not senise i Confommalon aad acivaor toswburate charge to substrate charge to substrate = Strucue of ery *Can consist OFT subunit with T |» Usually 1 subunit wih Tacve | Mult enzyme wi TaRGie actve ste sie active stes © Presence of oR binging of substate to active ste 'Can bo a multineric enzyme with + Has mutiplealostrc sites ‘mutiple subunits, each wah an (© But, Binding of 1 inhibitor ale ste acinar tufient hist ‘ectvate the sctviy of the enzyme tft of “hibéor 7 aaivator”on |= inhibitor structurally similar to | » Tnhiblor not sruchuraliy T+ Tatbsou Aaivatar snot enzyme & the ate of the enzyme: | substrate & hence "binds | ” similar substrate & hence binds |" tineaan tna Sobate & atalysed reaction reversibly 10 active site of] toasiteotherthan theactive "| _ hence bind to allosteric sit enzyme > This resus in eanfomationa | Hence inhibitor competes, with |-> This rosuts in a conformational | ~ cnange in ence Substrate for cine ste of |“ change in the enzyme active | >Binding of shblor stabilses enzyme ste, ‘enzyme in an inactive sate 0 Tis reduces the avaiabilty of > Thus substrate cannot bind to | Thusthe ate of easton’ ses ‘active. sites for substrate | acive ste Binding. of actwatr stabilses Binging + rate of reaction Yes ‘enzyme nan active sate kL > rato of rection decreases “Thus the ale of reaction sos Elfed “of 7 [eubaiae]_on We | At high [substrate substrate Te | > Tnnibior binds elle ther than innibtion ‘more likely to bind active site | ” active ete and changes the than the itibtor to form enzyne- | conformation ofthe active site substate | Hence the intr effectively }>Hence the same Vmax can be |” decreases the avaiable reached at high [substrate] [enzyme asi forms an }> Thus the effects of inhibition | _enzyme-inhibitor complex canbe overcome at high | Hence the effects of the (eubetratey inhtoton eannot be overcome by increasing [substrate] Graph demonstrating elect of >The enzyme ely osciates Inhibitor activator ‘between the active form and the inactive orm, > When the activator binds to {the enzymes, the active form Is slabiteed > When te inhidter binds to the enzyme, the inactive form estat lsvnetmanatesane | avmacdoowane Sree oo a] oath ‘EES a 3 i oT a Ta BS hl Speer in 2acpeaean nasa, : ste ne a tee | ae > pie ——b aman Bb -—---- on resent early in the pathway by | honing) Enzyme 2 Enzyme 3 Eiaty 8 cect cam oo Cora Sarina Bend ‘ {soloucine binds to afosleric se of enzyme actve ste of enzyme changed, no onger binds To tnconine "Nol AthoUgh enzyme nibion can bti be reverse & reversible, we are mote concerned wih reversible Tahiblors i our 3abus repared by: Mrs 5 Nair & irs Wee SH Rates instation (56) 4Na: Substanes pass between nucleus & ‘epic vite nuclear pores, They are "neo nuaoobdos & enzymes (rDNA ‘eplation &ransaapn), proteins (o make Up ibosomal subunits) which enor be eae 2) fORINA INA and lage and smal bosoms ‘buna wich lave he mleu] Rough ER ‘Smoeth ER ge aa SS eh fetenedcistorae tubular citomae AA |The RER and SER toga acts the ‘mombrane focry a the cel by acing ‘membrane proteins and posphotpis ots own ‘menbrane 2 Protein channels on the RER surface + Hold ne rbosome tn postion + low the entry ot poypepties sythesised on tne ibocomes on the euracs na he un es a vain oe oe ot =—& Zn ‘ci toce Qe nena Desenpion Function Nocieus ‘To contain to horediary mata 2 Raia phere TH] * Tocantot cet activites oy synthesising a ‘mRNA wich wal be Cancale a eukaryote cot ‘+ Surouded by a nuclear envelope (2 ‘double membrane) which perforated ‘ith pores & continuous with RER | + _ Contains te cteolus& chromatin Protine wach are neaded in thecal Naieolae + Non mambranoue, apr wba To synthesise RNA, a component of ‘bosomes ‘Assembly of large & sma ribosomal ‘Suburi sing ANA sythesoed | ucla & proteins exported fom ‘plasm + Hevediny staat oe + Artin, elongated threads of DNA Caled around stone proteins + 2iypesofervomatn ae present 4. Euchvomatin igh tine, ‘wanscptonay active, exsts ina toed, extended sis) 2. Heterochromatin (a stained ‘ancciptonalytnscve, ust found long th edge of nies) ‘Consists of tie RER & SER Rough ER (RER) + Anew of membranous Natlened ‘fas caled claternae + Has ribosomes ataced othe outer ‘irface ‘+ Continuous wit te outer membrane ofthe nuclear envelope Totransportof proteins which are syniested bythe nbosemes on Stace othe Gop soparatus va ‘Wanepor vesicles “Toallow proteins to fld into the native conformation ne citemal pace & ‘iyeonyate nem | Siooth ER (SER) +A etwor of membranous tubular sae ‘ald eiternae + Lacks ribosomes 0 outer euace (Singular cisterna, Puratcistemae) ‘To synthesise lpi and carbohydrates ‘To detoxify drugs & potsons (hus SER abundant ver) 7 Wanivane bound tioned sacs caled clternae & assodatod Golg estes + Consists ofa Yorming’ ores face wher new astra ae bing formed Dy fsin of vanspert veo rom ER. {@amaturing’ of trans face for spiel veses ona bt [NN = cance vac coraiing hydric | enzymes Ne: The artic enzymes wok best inthe ‘ck envionment of to ysosme. Ths 2 ‘yeosome burt, the enzymes are nt vey tive as tho cjtove has anew PH However, many ysesomes burt ten the cll be desvoyed | “To digest atrial engulfed by ie cal | To avcosyiat io pois ad is To farm gyeoproeins nd gyotniss To modi existing slycoprotains and alycolipids by mozivngiceaving he | (sng sugar chan ‘Toor and package protein ito diferent vestles and target to proto aileron, Dats of tocol arr secretion, TToterm Wsosomes To syntheses polysaccharides such as pci wich Wanspored in vesicles 0 Fre col membrane. (@regocytesis) ‘To reteate enzymes fom eats To digest unwanted or worn-out ‘organelles (autophagy) ‘Toell-destruct a col ater ts death (autiyss) Prepared by: Ns Sevamanl Nar aie ination (Vr 5-5)Coil Sovetare nai 3076 Sais Taian a + Sanna To apa ass —| Rose we oan sage Samad ys Gomsemanrane |" avec epson ges tray "yoowtrenirmecenern | beamnarete perp 2 Belimer mentary $n ocho mbes My le Comauindwninclangesies | "hasesanenctncsrrcrs ete tro ects psparion kel + sateen wonaes he aumonontal mati tesietbe ee ce imams space ek resrson oes oye Tt ene | Sinope nt mati |auimarimemorne | |* Sine ee | ane "ibosomes, phosphate granules & crags fs nse spain eae + Erte compl tre Coma a She pore) tmonan procs no maa 7 ad ara eanSaibd By [> — Gos Soa RANT tub ems rctocr cnr ety on + Wome cioapostzanitenat | Soughpmcrytiee ser mae nAm 8 rensomes Iremonnesycomicrcorscrat |‘ Stottghedopendet actons i ene ‘Skane sated thas Gece marae aR accepts onan) Sogo) wich ors a ioral ianca etd moteine + Fulguannchopaesumowsng te | 2)Stesfghtindprndet acon (tana cated stroma (conti Gahin yee) wach occurs ne stoma Sle eres, | F i 5 ye Sach gs) ace, oh its rani Et coe |. Siopnmaeetiar ween | Sachets atc BN es virgins |" Surman tera eth ensootnt sls “panama Cece cere | ecctmsseeatneastees ae soneane |° antl wei woman? | macho nds sopen eg Conboy nd Description + Consists fasmallEalarge subunit [+ Act as eae Yor prin Sythesls ae $ Acomplex of protein RNA May be found ntact rely floating a seal subunit (408) Ihe cytosol or bound to ER (or outer = ‘mombrane ofeuctear enolope athe | INB: Free sosomes produce prusine. that large subunit (608) ER coniavous withthe musear | funtion” wihin tho. efocol whl bound ‘ewoloe) during tansaton. The smal | fosomes” syhasce protens meant for {Farge sabunit ony come ogee | nserton ito’ membranes, packaging. win ug vada organise sooeion otal = oi cnn aig TT + To sta tlt rganng cone a tilt ot trot ofmicrites (tow uses |” QuTOC) doy spn ommoe cor fe tra ofp i each a hi = @, |. a Aa Oo peracetic ; + Founseampon caste remove open eas fe ip ee nvorome ich ioe ty ysl da i Sroanig conte nia at bbe ase LJ) coe econ costae Le Shine ses (ne ow maou Stes tococn Moots) ‘tire shen ‘ain’, alsa sort ‘The endomembrane system consists of the nuclear envelope, rough endoplasmic reticulum “smooth endoplasmic reticulum (SER), Golgi | pparatue (GA), eosomas and various vesses andthe plasme enbrane, DNA ransorbed nthe nutes to mRNAD mRNA leaves the nutes via the mucear pores>mRNA fs ranslatd ino polypepies on the roosomes ofthe RER-> polypeptides enlr fe ken of he cstoma ef ho RER where t undergoes madeabon> anspor estle use of fom fe REF ad ‘ary the proteins tothe GA ves fuses with tho cs’ ace of the GA and the protons undergoes fer medication, sting and Packing >a Secelory vesicle containing the prosn wil ud off fom the "van face of he GA and be transported to snd fue wth De cl suace memorane, ‘eleasing the prtaincortont of Be ves by exoeytaos, Microtubule ret the movement ofthe transport vescie to tie GA and tw secretory vesicle fo the cell surface membrana, Explain and dtingulsh betwen resolaon and magnification ‘Resolutio: The mnmurdstance whereby two pnts can bo seperated and llbe distinguished as wo pons. gnificadon: The degree to wich the vewed image fpr than he specie. ‘M: Mognincaton :Lenath of drawing =X (NB: temalos division of eyepiacegraicule under Low Power (0 bjecive) = TOam ‘Length of specimen ‘smallest vision of eyepiece graticule under High Power (40 objective) = 254m) (nts usualy used i miele) “Kner (F¥ ont) Draw plan dlagrams of tssues and calculate linear magnifications of drawings “When mating drawings emomber, STAMP [Siz of eran ust occupy 23 of given space 1 Tite must induce : plane of sacton, name o specimen, namo of suo calmagueaton eg. T'S. of epidermal eof onion (LP) ‘Annotation e..eoplas sats pullaway fom cl wal (nt ust eon) 4 tegalation 12. Cel wal cannot bo too ick when drawing a plant cel ust be proportional to he rect of he cl “Tipsy Savant Wale Raifos ination (Wr 65) z“Cataiar Functions Cal eniranes 2015-2076 ‘Stour ce 3 Rite ave a td morse mde! stature “rat tees ie mnarane mami thro were photphis & prin ae ao move {inte cn move bth tray & vancraey pop whe prtsns veal dv eat Taran between be Homes) ai becaae eth random aang pein one ae bean na phapi Beane \ nieces matin ycoorsin : cartohydate state recreate Sanat ‘Stoo Frome tae Prat eoarote HR . ‘caramantcan ann! protin Gert regs pte) fs {reo oer mowomert of ‘Sosa por olson’ Campane | Carnie cals Slayer | “a-ha tyro meget ee eo bhoapa heat 82 yopt tomo arcu te 3 nee feuates the movement of ences io 8 at te ent 2 ghewaiticlone nero acing abs barter to move los ear ad roe -Maneueeus emement.tey amaegeto | maleaee ‘oma pocooi bay sae he {37h charge, polarty ands of mote nent aby pass Posphatcheaaii wins pqvoous | frog he al nase neces of wsctraca aes we {wc sate hyorcaoon its eema | wank wi afte ha Soe ee ‘rdropobi core nth ora be ayer ‘Cases [Faun bene csp mcs) “Clea egos marian Ty Te FEDS SEE Tronure:oanaroos ‘te manivaels pevorted fob oy owas omgroaes -Rava chance ag sactre 2 cles esis pes moremen too ios wah Sight anna oo ths» ie posphonse ‘wcrophle pola, hysony group 2 | > The mantane peered fom bing ovty fm aor eng at poropobit geese, Chast evere the cove pos Fspeobls a Noe Thetydonlgupofchoeceoatgnswin | pavens wkdicaietannen the clrged pena este the ~ Cio stabs ne ye ue vn et Ws nrons photo woe etait sued |” Sewer i se insure snd es ane [Renyaropost core cine man : a peroherd ‘} chanaProtine -Have dona at we nerophontas win | + se tamnrembrane pote ep ap) & hyphae wih pl | > may begin, whch sna ey can open aw edits of wuts rctaned on Siti cn be new pron ations steels wregte ‘hes este mabe, iremovenentat ute 0.9 votap aad Ne canteens > may ale gate oms on open pssngeoy tere et tis of ‘asermolies sccm he menoane fom sign ow ate concauton og. saponte 2 Garr Poti fate ates confomatons) we + tnd he Soo on one sie be marorane a a su he pot Nanpon acess mentrnesswtttoacat, | "unsenoesa conformal shane hetaons seomrelne soe vee ‘o| sBesreniSetemensone v9 pester grzain of vst ich a usa 1 | ene te pane al nny ee RTP bro ope ‘obi namenia at encetaon grain rom ow sae concansiar igh sete 2 Thamar be seston nsaentt | Tm shove wo pes Shin senna fr caged whch ces a estoy sata | Tews wo pps of rts ncaa fr be never. Fea cy a ae ee Ee pe | mics eg wap ees as eae ore Ceres on pr mks coh poche he yea e oe he 2) ft te maiteranceo fonk_araents| Freon a ensymes (0.9 actconertose wich ae oud on ot stata cl 10 Wat pues can be | syapicmemtane yes teunboncnon seavcnooey nent - Plate receptor protein (eg ut can ich spec and — ‘il. The maton fe igna ecg comple ht ah ” te rnin of ssid rts | racer ain ascate bral tacicany : ‘ieh_25_hosmanes ° Function to stabilise membrane structure as they are non-covalently bound Eegeponm 2 aan Boos obese | “Pendants &onrchis rae omer Ba Sieraee | Cay cate IC ae ‘AS i egal a meme pes Turco os mareraecognion sesh celcl ecagilon ad ‘Gin Carer enans aaCaE aac wi —| sation Tanga to mene (ole 129s cols beatae one ancer frm ses an eas: hosp had -Functon sree | ealereoa chem ts tomanes Prepared by: Mrs, Selvaneni Nair aifesistalton Wr 58) Z‘Cellar Fanetons eaten 215-2076 aa 1) Membranes ae 2 partly permeable barir which act ssa boundary) between iste and ouside of cal, ) between erganale snd “ofoplasm (9. Gol apparatus & cones) & (c) belw.conpariments win an organel(e r@ochondal mate ermembrane pace), 2) Membranes alows fr compartmentalisation which alow (unique environments io be formes for Highly epeiaed activities (ecg scxc envronmantin yeoaomes fo hyaic enzymes t wok) (‘Spatial separation of Bochemica processes & tus ther sequential operation win ace (€4, poten modification RER ana futher ren modesten, sorting and packaging inthe GA) (accumulation oftns te ighcanoontrabons (©.z.accumuaton of high concanraton of Hine intermembrane space ofthe itochonda enable a proton gradient to be established for ‘chemosmos) {5} Membranes act as surface for chemical reactions fo oocurin a sequent manner "> membranes may have uneionaly-reiated pons grouped togeer so thal sequent biochemical processes can occur (G2. the thylakod membranes of he chloropiast have slacron cas & ATP eyncase fr chemumosts to sun) 4) Membranes increase surface ares for chemical reacions (@49. nner ritochonal membrane shy folded to old moe electron transport chins and ATP synthetase) '5) Memtranes ste oponaphy enable smmmurication ef ce! wih torancigs ‘2 he unique combination of proteins/gcoprteinspyotpids on srace of ferent cs enable {@ cot-all recogniton end saheston So that asus Yormaton poss (viruses to recognize and nfoct hoe celles (@)igands orecognted spect receptors so tha signa ranaduction can occur Tan | Movement Type ot | are eros Piece | iow | Pie Something to note ifasion | ns no ete: Wt mavemont of mis. ors Tom 3 conconraon, 29. 0, tendency for water molecies to lave a soln. In pant cel, wate potent depends on ‘ie exten by which deslved sole loware water poe ie te sole potenti 2) pressure exerod by th cl wall pana he cel face membrane Ia. pssst olen Wiotc potenti ofa place ==‘ potent fed contents + pressure potent fc wal a os We ‘The St untie Pascal (a). Water potent of pure water zero. This the maximum for water potenti. ‘When we add slut, () Ye becomes we (2) conconraton of out nreases ‘nen we add moe slate, () 9, becomes more ve (2) concanaton of ait creases more Vien we add ovenmore olde, (1) ¥abesomes even mow-vo ‘2 concetation of soit creases ver MO + Atinciplent plasmolyss, y= 0. Thus Wa « ws > De plasra membrane just sats 1 pl away from the cl wal + Netwater movement occurs rom 3 region of high wala poten a repon of fow water potential down 8 water potential gradint. —repere by firs Sevan Nair ‘as ation 6) 21. Oiganelle synthesis occurs nthe Gr & Gr Paces, 2. DNA replication ocr dung § phase 1 Chromatin tveads condense. Each ‘chromosome svisble 35 two ster {romatisjlned atthe contomere 2. Synapais occurs, homologous ‘romosores pal upto fom bivalents 8. Crossing over occurs between non-sster chromatids of homologous cromosome ats, arming. chiasmata (ates of {xossing ove), Corresponding segments ‘of nonsistr chromate are exchanged 4. Centos migrate to opposie ples ‘nd sind fves extend from each pole totinotochores& metaphase pale ‘5. Nuclear envelope diitegrates 6, Nucleolus wsappeare 1 Kinelochore meubules algn homologous pairs atthe equator nfo rows with cach 1 Kinetochore microtubules shorten and ‘homeogues are led by the centromeres {0 opposte poles, Non-kinetochore microtubules elongate causing the 2 poles {fo move futnes "Each pole has 2 haploid eat of chromosomes. 2. Chromosomes uneol into chromatin 3. Spinal bres dcntegrate 4 Nuclear envelop reforms around the ‘hromosomes at each poe & nuceo ‘O10 davaiee cas ru 1. Chromatin tveads condense Each chromosome vile 28 tw sister mats joined bya contomore 2. Centos cupleate & migrate o opposite poles. Spindle flores exond fom each pole {okinetechores & metaphace plate 2. Nucear envelope esitagrates Nucleols dappears 1. Kinetochore mrolubues algn chramesemes ‘atthe equatorin one row The ointaion of site chromate af each ‘quomosome f comoleehyinependert of ' Centromores of each dorceome divides 2. Kinetochoremiretiules shorten & pul he ‘Str chroma (ow cad cromosomes) centromeres frst to apposte poles. Non- Kinetochore mlerotubutes elngete casing tne 2 poles fo move tutes apart 1. Chromosomes uneod into chromatin 2 Spindle bes disietegrate 53. Nuclear envelope reforms around the ‘tomosemes at each poe ofboth cas 2162076 ar Tigeeocceen eee @: 2, Bu epson car eg phase "Chromatin tweads condense. Ere chromosome is walla as bo ster chromatids Joined atthe centemere a MEIOSIS: MITOSIS | 2. Contrcies marae to opposite poles & spine ‘res extend om each plete kinetochores & B metaphase pate 3, Nuclear envelope disintegrates 4. Nucleus dia 1. Knetochore microtubules aogn cromosomes atthe equatarin one row. 1; Gentromeres ofeach chromeseme etree 2 kinetochore microtubules shorten and pul the sister chromalis (now ealee ‘vomosomes) centromeres fret o opposite poles. Non-kinetochore microtubules congo ‘causing te 2 pols fo move further aban, 1 Chromosomes uncot nto chromate 2 Spindle fores dentegrets 3: Nuclear envelope efams around the chromosomes at each pola & nucleo reappese ‘Animal coli: Cell membrane invaginates towards the mace, forming 8 cleavage furrow, Cel membranes jin up and neparte the 2. ‘daughter cate Pant cells Vacuoles appear inte middle of he ‘el They coalese to foams cal plat, separaing the 2 daunter ces * GEER contains one complete set of chromosomes e ‘0. contains half the number of chromosomes 2s a Spd Cell contains one member of each homologous pair of cemasomes Le, one chornoseme trom ether parent) + BISBEE Sette comes ot vomonanes {e. cromosomes exst ax homologous pals Each set of chromesomes is rom one parent ‘> have same length, contromere postion &stainng patio ‘cary genes conting the same lnheted enaracereics a the = foci on both members ofa homologous pa ‘onesponding| : one sof matemal ogi + ona of patema rn Q ®) |, Henco each member af a paris genaticaly dren om eachother 27) | > pai upto fom brates during prophase tof meen, ‘Thus athough each member ofthe homologous pa may have genes coding forthe sme characteristics (€9, ee calou? at coresponding lc, they are ‘eneticaly ferent form each ater as they usualy have diferent ales (6. alle for be eyes & for green eyes, each of which have diferent aucecise, sequences fr each of the characteistcs. "2 220 te result of DNA replication and hus have the samme alee ‘> are genetically identical before erosing over occurs bebween no. siber cvematés) "@@| eG se @@) wet s)ra *Q: Whatis the ciference between chromosomes & chromatin? ‘Chromatin: Complex of DNA & proten ‘Chromosome: 1) Uncondensed form > a mass of lng, hin tead-ke fibres of chromatin 2) Condensed form > chromate that has been condensed by cling and {folding many tes upon itself & appear shor. tick structs Rates Insuion (Vr 56) 7