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Biochemistry Review

Biochemistry Review. Melissa Allen, Hilary Alterman, Jaimie Bandur, Tim Bender. 3.1.4 Draw and label a diagram showing the structure of water molecules to show their polarity and hydrogen bond formation. 3.1.5 Outline the thermal, cohesive, and solvent properties of water.

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Biochemistry Review

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  1. Biochemistry Review Melissa Allen, Hilary Alterman, Jaimie Bandur, Tim Bender

  2. 3.1.4 Draw and label a diagram showing the structure of water molecules to show their polarity and hydrogen bond formation. • 3.1.5 Outline the thermal, cohesive, and solvent properties of water

  3. Diagram of Water Molecules

  4. Properties of Water • Cohesive properties • Water molecules “stick together” • Affects different living systems • Allows insects to walk on water • Allows for water transport in plants

  5. Properties of Water • Solvent properties • Water molecules are polar. They are attracted to the strong ionic charges of the ions in the solution. • For example, Na+ ions exert a strong attraction on water molecules, forming shells around the ion. • This causes ions to isolate from one another. Process is called solubility

  6. Properties of Water • Thermal properties • The hydrogen bonds allows storage of kinetic and potential energy • Water absorbs a lot of heat before there is a change in temperature, therefore making water a useful substance for living organisms to utilize

  7. 3.1.6 Explain the relationship between the properties of water and its uses in living organisms as a coolant, medium for metabolic reactions and transport medium.

  8. Relationships • Cooling effects • The heat generated by the body needs to be removed to prevent denaturation in enzyme systems • Water absorbs a great deal of energy before becoming vapor • Effective agent for heat removal & maintaining body temperature • Blood (composed of water) can absorb and carry heat away from hot parts of the body to cooler parts.

  9. Relationships • Medium for metabolic reactions • Water is a universal solvent • Substances are easily broken down • Example: water helps break down NaCl by forming a barrier around the Na & Cl by separating the two

  10. Relationships • Transport medium • Water is a solvent in blood, tissue fluid, and cytoplasm • Water allows soluble minerals, carbohydrates, and amino acids to be transported

  11. Identify amino acids, glucose, ribose, and fatty acids from diagrams showing their structure. Be able to sketch each one.

  12. Amino Acids

  13. Glucose

  14. Ribose

  15. Fatty Acids

  16. 3.2.3 List three examples each of monosaccharides, disaccharides and polysaccharides.

  17. 3.2.4 List one function of glucose, lactose and glycogen in animals & of fructose, sucrose and cellulose in plant. • Animals • Glucose - blood sugar • Lactose - milk sugar • Glycogen - energy storage • Plants • Fructose - honey, fruit sugar • Sucrose - plant sap • Cellulose - cell wall structure

  18. 3.2.5 Outline the role of condensation & hydrolysis in relationships between mono-, di-, and polysaccharides • Monsaccharides form glycosidic bond to form a disaccharide, more bonds to form a polysaccharide • Fatty Acids: 3 fatty acids + 1 glycerol. 3 ester bonds = 1 triglyceride • Amino acids- peptide bonds, dipeptides or poypeptides

  19. Condensation reaction of amino acids to form a dipeptide

  20. 3.2.6 State 3 functions of lipids • Concentrated sources of energy • Waterproofing • Waxy cuticle in plants, feathers of ducks • Cushions and absorbs shock to protect organs

  21. 3.2.7 Compare the use of carbohydrates and lipids in energy storage

  22. 7.5.1 Explain the 4 levels of protein structure and indicate the significance of each • Primary- Sequence of amino acids with peptide bonds. Redefines final shape based on chemical interactions • Secondary- Shape of polypeptide: alpha helix coil or beta pleated sheet. Uses hydrogen bonds • Tertiary- Fold of proteins due to reactions between R groups: disulfide, ionic, hydrogen bonds, and hydrophobic interactions • Quarternary- Polypeptide chains: different groups have different functions

  23. Globular Can be single chains Easily soluble in water Tertiary structure critical Round shape Can be catalytic, regulatory (hormones), transport, protective (antibodies). Insulin, hemoglobin Fibrous Parallel polypeptide chains in long sheets Long shapes Only in animals Water insoluble Tough, supple, or stretchy Structural or contractile role Collagen, actin and myosin 7.5.2 Outline differences between fibrous and globular proteins and give 2 examples of each

  24. Explain control of metabolic pathways by end-product inhibition • Prevents cell from wasting chemical resources and energy • Assembly line process • When end product is present and in sufficient quantity, the process stops

  25. End product binds to allosteric site of the first enzyme • As the existing end product is used up, the first enzyme is reactivated

  26. Inhibition • Competitive • Prontosil • Binds to enzyme for folic acid • Binds to allosteric site and changes shape of the enzyme • Non-competitive • Arsenic • Binds to sulphydral groups of the protein, destroying it

  27. Enzymes lower activation energy • Enzymes are catalysts --> speed up reactions • Influence the stability of bonds • Provide alternative reaction pathway

  28. Induced Fit Model • Enzyme or substrate changes shape in order to fit • Substrate becomes bound to the enzyme by weak chemical bonds • Shapes return to normal after the reaction

  29. Metabolic pathways consist of chains and cycles of enzyme catalyzed reactions

  30. Use of lactose in production of lactose-free milk • Lactose is a disaccharide in milk • Made up of glucose and galactose • Some people have lactose intolerance • People who are lactose intolerant can’t drink milk if it’s not lactose free • Lactase --> enzyme that digests lactose into glucose and galactose

  31. Effects of pH on enzyme activity • Different enzymes have different pH ranges • Enzyme activity will increase until optimum pH is reached • Enzyme activity will then decrease because the enzyme denatures • Bell curve

  32. Effect of Temperature on Enzyme Activity • No activity at low temperatures • Enzyme activity increases as temperature increases • Once the optimum temperature is exceeded, the rate decreases because the enzyme denatures • Bell curve

  33. Effect of Substrate Concentration on Enzyme Activity • Enzyme activity increases as substrate concentration increases • Rate plateaus once all of the enzymes are in use

  34. Functions of Proteins • Structural • Collagen • Regulatory • Insulin • Contractile • Myosin • Transport • hemoglobin

  35. Significance of Polar and Non-polar Amino Acids • Polar --> hydrophilic, can contact water • Non-polar --> hydrophobic, can’t contact water • Lining of protein channels is polar, so it allows for diffusion • Polar amino acids allow for the positioning of proteins on the external and internal surface of the membrane

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