JMOLECULES |) ‘Al living organisms are made up of the same elements and compounds, If we perform an analysis of a plant tissue, animal tissue or a microbial paste, carbon, hydrogen. oxygen and several other elements are obtained. The same analysis mace on a non-living matter tke a piece of earth's crust, gives a ist of similar chemicals. A lose examination reveals that the relative abundance of carbon and Hydrogen with respect to other elements ts higher in living beings than in carth’s crust. HOW TO ANALYSE CHEMICAL COMPOSITION . Various biomolecules present in a living tissue (ike a vegetable or a plece of tive) can be studied by their chemical analysis. . To avg tse and grin itn frchloroaestic acid C,CCOOH using a mortar and pestle. We obtain thick sherry. + When we strain this shiny through cheese cloth or cotton, it gives two [ractions. * One ts caled fitrate or acid soluble pool having thousands of organie compounds, + Other fraction is called retentate or acid insoluble pool containing proteins, nucleic acid, polysaccharides ete. * The acid sohible poo! contains chemicals with small molecular mass of 18-800 daltons approximately. They are called micromotecules or blomicromolecules. They include amino aclls, sugary, nucleotihs etc. © Theacteinsoluble fraction contains organic compounds that have molecular weights in the range of ten thousand daltons and above. They are known as macromolecules or blomacromolecules. They inchde polysaccharides, proteins, nuclele acids, © “Lipids are not strictly macromolecules, their molecular weigh! do not exceed 800 Da, but they come under the macromolecular fraction becayse when we grind a tissue, cell membrane and other memibrances are broken {nto pieces and form vesicles which are not water soluble Oipids are also present in structures tice cel membrane and other membranes). “+ Theald-soibe fraction epesens roughly the etopasmic composition (thou organelle the ac insoluble fraction the macromolecules of the: and coll 3. The two fractions together represent the entire chemical composition of living tissues or organisms. Biomolecule-+ All the carton compound that present in living tissue, Biomolecule pee Micromolecule Mocromolecule (Mol. Weight < 1000 dations) er 1000 daltons) Present in ocid soluble pool ‘Present in acid insoluble pool Isa ea : Amino acids, N, base, Monosaccharides Protein, nuckelc acid, Polysaccharide are micromolecules but obtained under macromolecular fraction due to their insohible ‘acell. a EeTable : Average composition of oclls ‘Allcarbon compounds that we get from living tissue can be called Biomolecules. Inorganic elements and compounds are also present in the luing organisms which can be known with the help of ‘aah! analysis technique. ‘A small amount of a Eving tissue (e.g. Lea! or liver and this ts called wet weight] Is weighed and dried. All the water evaporates ‘When the tissue fs fully burt, the carbon compounds are oxidised to gaseous form ike CO,, wotur vapour are ‘temaved and the renant is caled ‘ash’. This ash contains many inorganic elements le calckum, magnestum etc. In the acid-soluble fraction - inorganic compounds lia sulphates, phosphates ete are also present Elemental analysts ghes composition of Ihing tissue in the form af ©, C, H, N ote ‘Analysis of compounds gives an idea of the kind of organic and inorganic constituents as mentained in the table Table: A comparison of elements present in nar-living and ving mater ma Mh tcc amma ocices res:aes Table : A list of representative inorganic constituents of Irving tissues. From a biological point of view we can classify the biomolecules into micromolecules and macromolecules. Water is the most abundant chemical in kving organisms, PRIMARY AND SECONDARY METABOLITES Living organisms produce thousands of organic compounds (biomolecules) including amino acids, sugars, chlorophylls, haems etc. these are required for their basic or primary metabolic processes like photosynthesis, respiration, protein and lipid metabolism etc. these are called primary metabolites. Many plants, fungl and microbes of certain genera and families synthesize a number of organic compounds (biomolecules) which are not involved in primary metabolism and seem to have no direct function in growth and development of organisms. Such compounds are called secondary metabolites. Thus, primary metabolites have idenlifisble functions and play known roles in normal physiological: ¢ucesses. ‘The functions or role of secondary metabolites in host organisms are not understood. However many of them are useful to human welfare (e.q., rubber, drugs. spices, scents and pigments). Table : Some secondary metabolites eee COMPOUNDS OF PROTOPLASM. ‘Although some elements occur in protoplasm as free lons but mostly two or more elements are variously combined to form diferent kinds of compounds. WATER : a Iisa best sokent in nature, it forms the fluid matrix of protoplasm. All other constituents of protoplasm are its sohtes. It itself participates in certain types of chemic=! reactk: particularly in the hydrolytic breakdown of complex compounds. Of total water, 95% water is free waler and 5% water occurs as bound water. In animal kingdom - Hardest material ; Enamel In plant kingdom - Hardest material : SporopolleninPre-Medical SALTS: ay ( ‘These help in formation of linkage or chemical bonds. Such type of linkage is called as “Salt linkage”. Some ions also act as co-lactor = 21"? —-Carbonie anhydrase Cu" - Tyrosinase [CBSE 2004] ‘Some other functions of tons : Ca"? ion. - Blood dotting, Bone formation ~ Mest abundant mineral element in animal body ORGANIC COMPOUNDS OF PROTOPLASM : td 4 teed Main source of energy. First respiratory substrate ~ carbohydrate Compounds of Carbon, Hydrogen and Oxygen with ratio of H and © is 2:1, so they are also called as hy- drates of carbon (Generalised formula of carbohydrates ts C_ (H,O} y. (Chemically all carbohydrates are polyhydroxy aldehyde or ketones. Simple carbohydrates which are soluble in water and sweet in taste are called “Sugar”. are main source of energy in body. in a normal man 55-65% of energy ts available to him is in the form of carbohydrates present in his diet CLASSIFICATION OF CARBOHYDRATES ; ‘On the basis of number of saccharide units obtained upon hydrohsis, Carbobyrates are dassified as Monosac- charides, Oligo saccharides and Polysaccharides, They are simplest sugars which can not be further hydrolysed. In their generalised formula x is mostly equal to y .e. number of Carbon and Oxygen atoms same. First step of oxidation - Phosphorylation i ern has ce da erp te Dn sre 1 CeO 1 eee CH,OH Dihydroxy acetone 5. The structure of saccharides is elther ring or straight chain. 6. Asixmembered ting ls known as pyranose and five membered ring is frances Pyranose and luranose names were given by “Haworth.” ance rico ti7. Anomer = In aqueous solution, Gucose occurs in cyeiic structure. In anomers of glucose, position of - Hand ~OH groups are changed on C, carbon atom 4—§ a-Glucose (Pyranose structure) 4 Reg 20H Gt0H q-o ie HO-¢-H MN H-C-OH RA musde. Glycogen {s ako called as animal starch. Glycogen is highly ‘branched polymer of 01 -D-ghucose. © Giycogen is formed by the 1',4° bond nkage in long chain and 1',6" bond Inkage at branching point. % Giycogen gives red colour with lodine: i Glycogen := Storage form of carbohydrate in animals, storage region of glycogen is liver and muscles. Glycogen is stored food of fungt | EOD OL. Diagrammatic representation of a portion of glycogen {@)_ Chitin =~ Linear polymer of N-acety- D-glucosamine with B-1', 4"-linkage. "N-acetyl D-ghicosamine is an amino acyl (-NH-CO-CH derivative of f-D-ghicose. S Chitinis an important component of exoskeleton of Arthropods and cell walls of fung) "Second most abundant organic molecule on earth. S _Inis ako called Fungal cellulose (e) Inulin = Linear polymer of fructose units inked with [3 -1".2" bonds. inulin is found in roots of Dah ita and Artichoke. Is water soluble polysaccharide and Its used to know the glomerular iteration rte, ‘A ini smallest storage polysaccharide ()—Dextrin - Dentrin is an intermediate substance in the digestion of ghoogen and starch. By hydrolysis of dextrin, ghueose and maltose are formed. It also occurs as stored food in yeast and bacteria. Heteropolyssccharide ~ (Composed of different monossecharide units (4) Hyaluranie acid = Found in vitreous humour, umbilical cord, joints and connective tissue in the form of hibvicating agent. Il also eecurs in animal cal eost as binding material (Animal cement) (0) Chondroitin - Chondroitin occurs in connective tissue. (2) Heparin = It is anticoagulant of blood. (@ Pectins - "Pectin is found in cell wall %S Saltsof pectin Le. Ca and Mg:pectates form middle lamella in plants. kis also called Plant cement. fe) Hemicellulose — tise stored material in Phytelephas (Ivory palm). Hemicelhilose which is obtained from this plant is white, hard and shiny and it is used to form bilard balls and artificial ory. 2sPte aA CMUCOPOLYSACCHARIDES Skimy polysaccharides with capacity to bind proteins and water are called mucopolysaccharides. In plants. mucilage isa common mucopolsaccharide. Special Points : 1 Peptidoglycan - Present in cell wall of bocteria. — Composed of N - acetyl Glucosamine + N - acetyl muramic acid + peptide chain of 4-5 amino acids: 2. Agar-Agar - It s.2 mucopolysaccharide which is obtained from some red algoe - Gracilaria, Gelidtum, Chondrus. tis composed of D-galactose and L-galactose unit (1, 3 linkage) and after every 10° unit « sulphate group is present. It is used for preparing suture medium, 3. Difference between gums and fevicol : Gums are natural mucoplysaccharides while {evical is synthetic rubber based adhesive. ‘STARTING TO CARBOHYDRATE 1. Which is not true about monosaccharides ? (1) reducing nature (2) sohuble in water (3) sweet in taste (4) always ketose 2. Glucose and galactose are two lsorneric monosaccharides known as = 0) Anomers (2) Epimers (3) Sugars (4) Amino sugars 3. Choose the mismatch : (1) Amylose -+ contains a-1,4 glycosidic bond. i (2)K: — most abundant mineral element in ICF. (3)Na* -» most abundant mineral element in ECF. {4) Cethulose -» violet colour with lodine solution, 4. Sum total of all the reactions that are taking place in a cell is known as (1) catabolism (2) enabolism (3) metabolism (4) redox reaction. 296 EeIM) rrerac anim anec uc rasecenannE TOON Fot and its derivatives are combinaly known as lipid. ‘Compounds of C, H, O but the ratio of Fiydrogen and Oxygen is not 2:1. The amount af oxygen is consider- ably very lass. Lipids are Insoluble in water and soluble in organkc solvents like sc¢tones, chloroform, benzene, hot alcohol, ether etc, Lipids occur in protoplasm as minute globules. Lipids do not form polymer. Lipids provide more than double energy 0s compared to carbohydrate. th animals, {at are present in subcutaneous layer and work as food reservoir and shock-absorber. Lipid requires less space for storage as compared to carbohydrate because lipid molecule is hydrophobic and condense ‘Animals store maximum amount of food in the form of lipid. Uplds are micromolecules. Lipids are caleds fats and oils on the basis of meting point, Oils have lower meting point and fals have higher meking point. ‘Some lipids also have phosphorus like lecithin. (A). Simple Lipid or Neutral Fate :- © ‘These-are esters of Jong chain fatty acids and alcohol. In majority of simple lipids, the alcohol is a trihydroxy sugar alesholl.e. gheeral Three molecules of falty acid inked with one molecule of glycerol. The linkage is called “estar bond”. Such type of lipids are called as Triglycerides. Three molecules of water are released during formation of trighcerides (dehydration synthesis) Glycerol Is also known as tihydroxy propane. ‘Similar or different fatty acids participate In the composition of a {al molecule. Simple lipids contain two types of fatty acids.Pre-Medical ‘© Simple lipids contain two types of fatty acids. (e) Only single bond, single bonds are present fal Doble bonds also present with single between C-C atorns bonds between C-C atoms. (0) Also known as non essential fatty acid, Alwo known as essential Fattyacd becunse because they can be synthesized in animal they can't be synthesied in animal body, body, soitis not essential to take therm with So It is essential to take them with food food. Lipids with more amount of unsaturated (2 Upids with more amount of saturated fatty iy cits ane meaty present i Und acids are mostly present in solid form at normal temperature. 9. Butter, Ghee Metabolicaly they are highly reactive, so (@) — Metabolically they are very less reactive. So mostly participate in metabolic reactions. mostly don't participate in metabolism. So ‘So don'thave tendency to store in animal have tendency to store in animal body and body. So no obesity, no cholesterol cause obesity. Some amount of saturated formation, no cardio vascular disease, 0 fatty acids convert into cholesterol in liver. high B.P. & no harmful effect. This cholesterol deposit on Inner wall of blood vessels, so cause high blood pressure & different types of cardiovasular disease. Mostly paint fat contains high amount of (fe) Mostly animal fat contains high amount of unsaturated fatty acids. saturated fatty acids. Examples No. of © Example Palmitic acd == 16 ‘Stearic acid = 18 ‘Waxes are monoesters with only one molecule of fatty acid attached to.a monohyiroxy alcohol og Spermacat! In sul of whale and Dolphin. (B) Conjugated or Compound Lipide =- (1) Phospholipids or phosphatide or phospholipins == i 2 Molecules ol fatty acid + Glycerol + H,PO, + Nitrogenous compound. Phospholipids are most abun- ; dant type of lipids in protoplasm, Phosphotipids have both hydrophilic polar end (H,PO, and nitrogenous compound) and hydrophoble i E non polar and (fatty acide). Such molecules are called amphipathic. Due to this property, phospholipids form bimolecular layer In cell membrane.[ih emer wcneoracimcucet ResecnsCUnne MOE ‘Some biologicaly important phospholipids are as following : fa) - toh i) Lecithin or Phosphatidyi choline Mitrogenous compound in lecithin is choline ‘code CH-O-P-0-CH-AH Misc, Phospholipid (Lecithin) CH, Cephalin-Similar to lecithin but the nitrogenous compound is ethanolamine, cephalin occurs In nervous tissue, egg yolk and blood platelets. ‘Sphingolipids or sphingomyelins similar to lecithin but in place of glycerol it contains an amine akechol sphingosine. ‘Sphingolpids occur in myelin - sheath of nerves. Glycolipid =~ 1 fatty acid + sphingosine + galactose Cerebroiside which occurs in white matter of brain Gangliosides - These occur in nerve ganglia and spleen. Derived Lipids = Lipid derived from simple or conjugated liptd . Derived lipids are complex in struc- ture. They ore insoluble in water and soluble in organic solvents. ‘Steroids : Steroids exhibit tetracyclic structure called “Cyclo pentano porhydrophenanthrane nucleus” (On the basis of furctional group, sterokds are of two types - Starola:~ Alcoholic steroids e.g. cholesterol - Cholesterol abundantly occursin brain, nervous tissue . Adrenal gland and skin. Cholesterolis a parent steroid. Several other biologically important ‘steroids are derived from cholesterol.7 - dehydro cholesterol which occurs in shin isa prositamin, ‘On exposure to ultraviolet radiation, t transforms in cholecaleiferol i. ¢ vitamin D Cholesterol ts also called "most decorated micromolecule in biology”. Cholesterol Sterones == Kelonkc steroids, for e. 9. sox hormones, Adreno corticoids , eadyson hormone of insects, ‘Chromotipid = It is also called terpene. Most complex lipid in protoplasm, Chromolipids composed of repeated Isoprene unitsPre-Medical - ‘ Protein name is derived from a greek word which means " holding flrst place" (Berzellus and Mulder) Essential clements in protein are C,H, O,N, Most of the proteins contain sulphur. In some proteins ledine . ton and phosphorus are present. After water, proteins are most abundant compounds in protoplasm. (7-14) amount of proteins. Proteins are polymerso! amino acids (Fisher and Hofmetster). There are approximately 300 amino acids known to exist but only 20: types of amino acids are used in formation of proteins R H-N-C-¢-oH rot if HHO Proteins are heteropolymers of amino acid. ‘Amino acids contain an amino group and carboxylle group on the same carbon Le. the a-carbon 40 they are called a-amino actds. Amino acids are substituted methanes. H wi, —¢—coon 4 Giycine Amino acids is amphoteric compound because it contains one acidic -COOH and an alkaline group -NH, t yo | H Alanine I COOH Ma Gon At isoelectric point, amino acid |s present in form of zwitter ion, NH zr-0-2 COOH == HSN- r-0-% Zuatter ton =coo7 == NHeC -Ccoo” 1so electric point is that point of pH at which amino acids do not move in electric lek Out of 20 amino acids, 10 amino acids are not synthesized in body of animals so they are must in dist. These are called Essential amino acid. e.g. Threonine , Valine, Leucine, Isoleucine, Lysine, Methionine, Phenylalanine Tryptophan, Arginine, Histidine. Arginine and Histidine are semi essential. 10 amino acids are synthesized in animal body so these are called Non essential amino acids. for eg. Glycine, Alanine, Serine, Cysteine Aspartic acid, Glutamic acid, Asparagine, Glutamine, Tyrosine, Proline Except glycine, each amino acid has two enantiomeric isomers COOH H-C~NH, R D-amino acid G00H HN-C-H R L-amino acid© — Most proteins have L- amino acids while D- amino acids occur in peptidoglycan of bactertal cell wall and antibodies, ‘Amino acids are joined with peptide bond to form proteins, -C-|OH +H] i 0 HN- a-O-= ‘+ — Peptidy| transferase enzyme catalyses the synthusis of poptide bond. ‘* _ Propertyal protein depends {1) on sequence of amino acid and (il) configuration of protels molecules, On HH SH ls ile eel an Hoon 4 }-CO-NH-CH-CO-NH-CH-CO-NH-CH-CO- Aminoacid Serine —Cysteine Spode — ie acid Sen (Cys) ™ = s © o Primary structure of a portion of a hypothetical protein. Nand C refer to the two termial of every protein. Single latter codes and three letier abbreviations for amino acids are also Indicated. i Classification of amino acids on the basis of number of carbaxylic groups and Amino groups. i: ‘Acidic amino acid nel ‘Thay have one amino and two carboxylic groups in thelr structure. | + [oh ernie ea (CH-CH,-COOK @g - Ghtamic ockd + H.N-C-COOH 4 ~ Aspartic acid v——_—_ i HtPei aes 2. - Alluline amino acid They have two amino and one carboxylic group. NH, AH, Frm = Fin, + Net charge = +ve, so they move towards cathode in electric field. ‘COOH coo” eg, Histidine Arginine Lysine Neutral AA They have one amino and one carboxylic group. ‘They are present in the form of zuilter jon and show no movement in electric field. eg. Rest 15 AA ‘Special Points on Amino ackd : 1 : ‘Tryptophan : Most complex amino acid and helplul in synthesis of LAA. (indole-3-Acetic Acid) which is. plant growth hormone. ‘Tyrosine : Helps in synthesis of melanin pigment, Thyroxine hormone, Adrenaline (epinephrine) hormone, Nor adrenaline (Nor epinephrine) Hormone. tn proline amino acids, imino group (ANI Is present instead of amino (-NH.) group so these two amino acids are abso known as imino acids. Cysteine and methionine are sulphur containing amino acids. Tyrosine Aromatic AA * Tryptophan |because they have, Pheny] alanine] benzene ring in their structure. _ Except glycine all amino acids are laevorotalory. Gicine is the simplest and Tryptophan is most complex Amina acid ‘Amino acids which participate In protein synthesis are called as protein Amino acids and those which do not participate are called as non-protein amino ackds. eg. GABA, Omithine. Citruline Configuration of Protein Molecule =~ wy (2) Primary configuration or structure = A straight chain of amino acids linked by paptide bonds form primary structure of proteins. This structure of proteins 's most unstable. Newly formed proteins on ribosomes have primary structure. ‘Secondary configuration = Protein molecules af sec. structure are spirally colled. In addition to peptide bond, amino acids are linked by hydrogen bonds between oxygen ol one amide group and hydrogen of another amide group. This structure is of two types - @ cr-Helts = Right handed rotation of spay cole chan with approximately 3% amino-acids in each tum. This structure has intramolecular hydrogen bonding |. e. between two amino acids of seme chain e.g. Keratin Myosin, Tropomyosin. |Mma 4 IM) Secemencc weimaracrrwcet nes scene] ACO AL 4 (i) B+ Heltx or pleated sheath structure ;- Protein molecule has zig — 229 structure, Two or more Protein molecules are held together by intermolecular hydrogen bonding. e.g. Fibroin (sill Proteins of sec. structure are insoluble in water and fibrous In appearance. ‘S _ Keratinisa fibrous. tough. resistant to digestion, selero protein, Hard nessof keratin is due to abundance of cysteine amino ackd in is structure. Tertlary Structure = Proteins of tertiary structure are highly folded to give o globular oppearance. They: are soluble in water (colloid sclution). This structure of protein has following bonds- (9 Peptide bonds = sirongest bond in proteins. (i) Hydrogen bonds ‘ti! Disulphide bond :~ These bonds are formed between - SH group of amino acid (Cysteine). These bonds are second atrongest bond and stabilise tertiary structure of protein. (¥) Hydrophobic bond ; Between amino acids which have hydrophoble side chains for e.g. Arornatic amino ocid {4 lanle bond : Formation of tonic bond occurs between two apposite ends of protein molecule due lo electrostatic attraction Majority of proteins and enzymes in protoplasm exhibit tertlary structure. Quaternary Structure ;- Two or more polypeptide chains of tertiary structure unite by different types of bond to form quaternary structure of protein, Different polypeptide chains may be similar (sctiedehy- drogenase) or disimilar types (Haemoglobin, insulin) Quaternary structure Is most stable structure of protein. gf Cartoon showing : (a) A secondary structure and (b) A tertiary structure of proteins Denaturation of protein :- Besides changes in pH, salts, heavy metas, temperature, pressure, ete. also cause Precipitation of proteins. Because of these changes. the secondary and tertiary configuration of proteins is destroyed. Such allemations im the physical state of proteins ts called denaturation. Il the change in the medium of protein te mild and for a shart peried, then denaturation of the protein is also temporary, however, if the change in. medum 's sirong and prolonged then denaturation is permanent and the protein becomes coogulated. For example, ‘the white or albumen of egg is a soluble globular protein but on heating it permanently coagulates into fibrous insoluble form. It Is dear, thal strong akemations result In the denaturallon of proteins and they lose their blolagical properties and significance. It is this reason, that cells of organisms are unable to bear strong changes and they ukimately die. 23TYPES OF PROTEINS Types of protein Simple Compound Derived (made up of only amino acids) Fibrous Globular Long, Coiled & Thread like 2 . ~ Present in chloroplast. Collagen s+ ~ Most abundant protein on the earth. ~ Most abundant protein in animal body - 1/3 past of tolal protekns Albumin = ~ Present in connective Misuse = Maintain BC.OP. ~ Threads of collagen known as Tendon = In mik as Lactoalbumin ~ In egg yolk as Ovalburnin Elastin :» = In blood as Serum albumin = In connective tissue T Fheseade of Eases se gir ‘Globin = Present in Haemoglobin. Keratin Histone protein :- Present with eukaryotic DNA, = Init Lysine & Arginine A.A. are present in more amount. Compound protein Protein part, Non: protein part ‘on azn acl pat Mode up of A.A. (Prouthetie group! ‘Types of compound protein on the basis of prosthetic group. * Nucleoprotein ; Prosthetic group ts nucleic acid. eg. Chromosome = DNA + RNA + Protein Ribosome = RNA + Protein Virus Chromoprotein : Prosthetic group is Porphyrin pigment (metal + porphyrin ring) ca Metal ‘Colour Haemoglobin Fe Red Cytochrome Fe Red Haemocyanin G Bue Lipoprotein : Prosthetic group Is lipid eg. Plasma membrane UP screenees setter are Pes RRR ERCo oe May ly Phosphoprotein = Prosthetic group is phosphoric acid (H,PO,) + — Caseinogen - Milk > Pepsin - Protein digesting emzyme. Lecithoprotein :- Prosthetic group is Lecithin €g. Fibrinogen - Blood Metalloprotein :- Prosthetic group Is metal eg, Enzyme with tts co-factor Glycoprotein :+ Prosthetic group is carbohydrate Oess than 4% carbohydrate) eg. (1) a, fy globulin of blood. Glycoproteins which are present on cell surface are hebplul in cell recognition, Human = Egg surface - Fertilizin - Glycoprotein ‘Sperm surface - Antifertilizin - Simple protein. Mucoprotein Prosthetic group Is carbohyirale (more than 4% carbohydrate} ‘Special Points on Protein ; Monomeric protein : Protein composed of ane polypeptide chatn Oligomeric/Polymeric/Muttimeric protein : Protein composed of more then one polypeptide chains. ‘Some proteins and their functions [Pons [Fences se Foe fear awa ° = GOLDEN KEY POINTS PR] tecrrscc wAuaraneuce fosemcnrcaese moots ‘Chitin is an example of Homopolysaccharide. In proteins only right handed hellx are observed, ‘Cellulose never show iodine test. Phospholipids are most abundan! lipld in cell membrane. ‘Thaumatine |s sweetest chemical substance which is obtained from Thaumafococeus danielll bacteria. ‘Aspartame/Aspartin is most commonly used artilicial sweetener, It is non carcinogenic .Pre-Medical BEGINNER'S BO! LIPID TO PROTEIN 1, The most abundant lipids in eukaryotic cell membrane are {1} cholestrot (2) alycotipkds (3) phospholipids (4) kpopolyssecharide 2, Which of the following is alkaline amino acid (1) glycine (2) valine G)alanine (4) arginine 3. Which biomolecule release maximum energy during oxidation (1) lipid (2) protein (B) nucleic acd (4) carbohydrate 4. Analpha helix represents {1) primary structure of protein (2} aggregation of protein (3) secondary structure of protein (4) tertiary structure of protein 5. Which of the following bond is/are found in tertiary structure of protein (1) peptide bond & hydrogen bond (2) disulphide & hydrophobic bond ‘@)ienie bond {4} all the above ee- FE Lhe Biology 4 NCERT BASED PROBLEMS 1, What are macromolecules? Give examples. ‘Ans. Macromolecules are large sized, high molecular weight, complex molecules, which are formed by polymerisation of condensation of smal sized, low molecular weight, simple molecules. ‘e.g. Protein, Nucleic acid and Polysaccharides. 2. Protein having primary structure. if you are gen a method to know, which amino acid Is at elther of the two termin! (ends) of protein. Can you connect this information to purtty or homogeney of a protein? Ana. No, because we know about the first and last amino acids, but in between them any type of amino acids ‘may present, for those we can not be sure. 3. Find out and make a list of proteins, used as therapeutic agents, ‘Ana. Proteins those are engineered in the laboratory for pharmaceutical uses are known as therapeutic proteins. ¢.q, Manodonal antibodies, interferons, Insulin, Erythropoetin. 4. Can you describo, what happens ? when milk Is converted into curd ot yoghurt, from your understanding of proteins ? ‘Ana. Denaturation (Coagulation) of proteins, present in milk, due to change in pH and temperature. & (Can you attempt madets of bomolecules, using commercially, avallable atomic models (ball and stick models). ‘Ans. In ball and stick model, ball is used for aloms and short rod.of wood / plastic is used to represent bonds ‘of 3 compound. 6. What are gums made of ? Is fevico! different ? ‘Ans. Gums are colloidal exudates of plant, which are chemically polyenceharide, while fevicol is synthetic rubber based adhesive. 7. Find out a qualitative test for protein, fat, oils and amino acd. ‘Ans. Protein = -> Biuret test + Alkaline CuSO, - reagent test “> Violet colour test Fat and Oils . Grease spot test -> A drop of all placed over a piece of simple paper, a translucent spot is visible. This Indicates the presence of fat. ‘Amino acids —+ There are different tes!s available for different amino acids. Ex: Milonstet | HNO, in HNO, i ‘Tyrosine and Tryptophan Xanthoproteic test | Cone. HNO, Yellow ‘Tyrosine, Tryptophan, Phenylatarine Briefly describe the bioinformatics. 8. Ans. Bioinformatics is the collecting, storage and analysis of large amount of blological data in computer, to make \seful conclusions. These data contain mapping and phenotype informations, nucieotide and amino scids sequence and structure and function of proteins. If) omen enuecmen noc permeate mot