2. Biological Molecules as a combination of monomer and polymer

Biological molecules include carbohydrate, protein, fat, water

1. Biological Molecules

2. Workplan Date : July 2 6 , 20 23 Subject : Biology Topic : Biological Molecules Activities Discussion of types of biological molecules

3. Question? What the biological molecule compos ing of our body? Making polymers from monomer  condensation reaction Broken down of polymer to monomer  hydrolysis

4. Learning Outcomes Students are able to describe the ring form of α -glucose and β -glucose Students are able to describe and distinguish monomer, polimer, macromolecules, monosaccharide, disaccharid, polysaccharide. Students are able to describe formation of glycosidic bond and the breakage of it

5. Biological molecules Carbohydrates Protein Lipid/fats Water

6. Monomer build up into polymer polymer  a long molecule consisting of many similar or identical building blocks linked by covalent bonds Monomer  small building-block molecules Isomer: Molecules that have the same molecular formula but different structures Polymer Monomers Hydrolysis

7. Carbohydrates Carbohydrates have the formula (CH 2 O) n Function: source of chemical energy for generating ATP needed to drive metabolic reactions; building blocks for larger molecules Consist of carbon, hydrogen and oxygen Ratio hydrogen to oxygen 2:1 3 major groups Monosaccharides Oligosaccharides Polysaccharides 3-7 C atom Short chain monosaccharides, most abundant  disaccharides

8. Carbohydrates Monosaccharides  the monomers from which larger carbohydrates are made , colorless Glucose, galactose and fructose are common monosaccharides . Has carbonyl group and hydroxyl group. Aldose or ketose Isomer: Molecules that have the same molecular formula but different structures Glucose has two isomers, α-glucose and β-glucose, with structures -OH on Carbon atom number 1 Macromolecules : Small organic molecules that c ombine together.

9. Monosaccharide colorless, crystalline solids that are freely soluble in water but insoluble in nonpolar s olvents C ontain from three to seven carbon atoms , names ending in “- ose ” witha prefix that indicates the number of carbon atoms , example: triose, tetrose, hexose. A condensation reaction between two monosaccharides forms a glycosidic bond . Isomers of glucose

10. Disaccharides T wo monosaccharides joined by glycosidic linkage Disaccharides can also be split into smaller, simpler molecules by hydrolysis Maltose  glucose + glucose Sucrose  glucose + fructose Lactose  glucose + galactose

11. Polysaccharide polysaccharide molecule contains tens or hundreds of monosaccharides joined through dehydration synthesis reaction Insoluble in water and do not taste sweet Examples: glycogen, starches, cellulose important structural polysaccharide is chitin  fungi, insects, spiders, crustaceans

12. Glycogen  muscles and liver cells, 1,4 linked α-glucose, branch on 1,6 linkages More branched than amylopectin Clump together to form granules Stored energy Polysaccharide

13. Starch  amylose and amylopectin amylose  straight chain (unbranched); 1,4 linked α-glucose  chain coiled up into helical Amylopectin , a more complex starch  branched polymer with 1–6 linkages at the branch points Polysaccharide

14. Cellulose  Polysaccharide

15. Research Structure The bond The example Additional : Lipid  structure of fatty acid, differentiate: triglyceride and phospholipid Secondary structure  α helix and β pleated Tertiary structure  4 types of bonds Water  the function Quaternary  globular and fibrous protein; structure of hemoglobin related to it function)

16. Exercise What is the different between 1-4 linkages and 1-6 linkages of glucose polymer and mention the examples. What the different between saturated and unsaturated fatty acid? Mention the funtions of the following lipids? Cholesterol and Phospolipid What is the different of structural shape between two polysaccharides starch and cellulose? Why does the enzyme that digest starch couldn’t digest cellulose? Answ

17. Exercise 1-4 glycosidic bond (linkages)  number 1 atom C linked to to number 4 C of second monosaccharide example: maltose, amylose 1-6 glycosidic bond (linkage)  number 1 atom C linked to number 6 atom C of second monosaccharide, example: amylopectin (it branches). 2.

18. Polysaccharides Most glucose monomere of starch joined by 1-4 linkages (number 1 C to number 4 C) Amylopectin  branched polymer,1-6 linkages at the branched point. Glycogen  similar to amylopectin but more extensively branched Fact: Glycogen can’t sustain energy for longer, glycogen stores depleted about a day (unless replenished by eating)

19. Polysaccharides cellulose  β configuration, making every glucose monomer “upside down” , no branched Microfibril  parallel cellulose held together “cable like”

20. LIPID Lipids make up 18–25% of body mass in lean adults . Contain carbon, hydrogen, and oxygen Proportion of electronegative oxygen atoms in lipids is usually smaller than in carbohydrates Group of lipid: Fatty acid, Triglycerides, phospholipid, steroid, other lipid (vitamin E, vit K) Fat  composed by of smaller molecules: glycerol and fatty acids

21. Examples: Red meat, whole milk, cheese, butter Plant: cocoa, palm oil, coconut oil

22. Examples Monounsaturated: olive oil, peanut oil, most nuts, avocado Polyunsaturated: corn oil, sunflower oil, soybean oil fatty fish (salmon, tuna, macarel)

23. Types of Lipid – Fatty Acid Fatty acids  Used to synthesize triglycerides and phospholipids or catabolized to generate adenosine triphosphate (ATP). Long carbon skeleton (16-18 carbon atoms in length )

24. Types of Lipid Fatty acids  Used to synthesize triglycerides and phospholipids or catabolized to generate adenosine triphosphate (ATP). Triglycerides  ( fats and oils) Protection, insulation, energy storage Phospholipids  component of cell membranes Steroids Cholesterol  Minor component of all animal cell membranes; Hormones (adrenocortical hormones, sex hormones)

25. Triglycerides Common lipid, known also as triacylglycerol. Consists of  glycerol + three fatty acid Ester linkage Solids or liquids at room temperature Fat  solid triglyceride at room temperature Oil  liquid triglyceride at room temperature Triglycerides are the body’s most highly concentrated form of chemical energy Deposition (stored)  adipose tissue (beneath the skin)

26. Phospholipid Phospholipid  glycerol backbone + two fatty acid chains attached to the first two carbons The head  polar (hydrophilic) The tail  non polar (hydrophobic) interac with other lipid only Componnent of cell membrane Steroid Steroids have four rings of carbon atoms , non polar, example: cholesterol Function: component of cell membrane (cholesterol), precursor of hormones (estrogen, testosterone)

27. Protein Protein : containing C, H, O, N; 12-18% of lean body Monomers of proteins  amino acids (20 differents amino acid) Consists of : an amino group (-NH 2 ); acidic carboxyl group (-COOH); a side chain (R group) Covalent bond joining each pair of amino acids is a peptide bond. Dipeptide ; T ripeptide ; P olypeptide As the peptide bond is formed, a molecule of water is removed

28. Peptide Bond

29. Functions

30. Functions

31. Functions

32. Functions

33. The 20 Amino Acid

34. The 20 Amino Acid

35. The 20 Amino Acid

36. Covalent Bond

37. The Bond forms when a hydrogen atom with a partial positive charge attracts the partial negative charge of neighboring electronegative atoms, most often larger oxygen or nitrogen atom

38. Structure of Protein Primary Secondary Tertiary Quartinery

39. Structure of Protein Primary sequence of amino acids that are linked by covalent peptide bonds to form a polypeptide chain

40. Structure of Protein Secondary Protein is repeated twisting (coiling) or folding of neighoring amino acids in the polypeptide chain Structure is stabilized by hydrogen bonds

41. Structure of Protein Secondary α -helixes (clockwise spiral) Β -pleated sheets Delicate coil by –H bonding between every fouth amino acid 2/more segments polypeptyde chain lying side by side connected by –H bonds

42. Structure of Protein Covalent bonds called disulfide bridges may Tertiary 3d shape of polypetide shape Structure is stabilized by hydrogen bonds

43. Structure of Protein Quatenary proteins that contain more than one polypeptide chain (not all of them do), the arrangement of the individual polypeptide chains relative to one another

44. GLOBULAR AND FIBROUS Fibrous proteins  polypeptide chains form long strands that are parallel to each other. ( collagen , elasti n, keratin , fibrin , actin and myosin ) Globular proteins  polypeptide chains are spherical ( enzymes, antibodies and complement proteins, hemoglobin, insulin, membrane proteins,

45. Denaturation protein encounters analtered environment, it may unravel and lose its characteristic shape (secondary, tertiary, and quaternary structure). This process called denaturation proteins become denatured if they are transferred from an aqueous environment to a nonpolar solvent .

46. Water Most of this water is in liquid form, water is also present on Earth as a solid (ice) and a gas (water vapor) The most important and abundant inorganic compound in all living systems Nearly all the body’s chemical reactions occur in a watery medium most important property of water, its polarity

47. Oxygen is more electronegative than hydrogen The electrons of the covalent bonds spend more time closer to oxygen

48. Cohesion of water cohesion  hydrogen bonds hold the substance together so w ater molecules stay close to each other Cohesion  water transport against gravity in plants Surface tension

49. Water as solvent Water is “universal solvent,” a substance that would dissolve all other materials

50. References: Cambridge International AS and A Level Biology by Mary Jones et al. , Cambridge Univ Press Priciple of Anatomy and Physiology 13 th Edition by Tortora and Derrickson, John Willey and Sons Publ. Campbell Biology 11 th Edition by Lisa Urry et al. Pearson