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Accelerated Nutrition Protein Unit Study Guide/Review Sheets Answer Key I GENERAL PROTEIN STRUCTURE and AMINO ACID CLASSIFICATION: 1. 2. 3. 4. 5. 6. What element(s) ALWAYS comprise proteins? C, H, O, N Are proteins organic? YES What element(s) MAY be present in proteins? S What is the name of the monomer of proteins? AMINO ACID What type of bond links amino acids together? PEPTIDE BOND What functional groups is shared between ALL amino acids (giving it its name..)? AMINO GROUP & ACID GROUP 7. What functional group on an amino acid differentiates it from, for example, a carbohydrate? R GROUP; VARIANT GROUP 8. Is the group from question #7 the same or different on each amino acid? DIFFERENT 9. How many standard amino acids are there? 20 10. How many (of the standard amino acids) can our bodies synthesize? 11 11. What are the amino acids that our body can synthesize named? NON-ESSENTIAL AMINO ACIDS 12. How many (of the standard amino acids) can’t our bodies synthesize? 9 13. What are the amino acids that our body can’t synthesize named? ESSENTIAL AMINO ACIDS 14. If our bodies can’t synthesize certain amino acids, where do we get them from? DIET 15. Why is it important that we have all of the twenty amino acids? IF YOU DON’T HAVE 1 YOU NEED TO MAKE A PROTEIN (THINK PRIMARY STRUCTURE) YOU CAN’T SYNTHESIZE THAT PROTEIN 16. What neutral molecule is formed when amino acids bonds together? WATER 17. What are the names of a molecule that has 100 amino acids linked together (two answers)? PROTEIN A.K.A POLYPEPTIDE “MANY PEPTIDE BONDS” 18. Explain how three different proteins can be composed of 50 amino acids. a. SAME AMINO ACIDS, DIFFERENT ORDERS (2) OR DIFFERENT AMINO ACIDS (1) BUT ALL CONTAIN 50 QUALITATIVE TESTING FOR AMINO ACIDS AND PROTEINS 19. List the names of the qualitative tests used to identify amino acids and proteins and list and draw the functional group(s) that it tests for. Ninhydrin Biuret Lead Acetate Sakaguchi’s Xanthroproteic Ammonia (NH3) or Primary Amine (NH2) or Secondary Amine (NH) PEPTIDE BONDS or 2 or more amides (N-C=O) Sulfur groups Guanidines Phenyl groups/substituted aromatic RINGS Any protein has to have peptide bonds ;) 1 Protein Unit Exam Answer Key II LEVELS OF PROTEIN STRUCTURE 20. Define the primary structure: THE SEQUENCE OF AMINO ACIDS 21. Describe the type of bonding in secondary structure and where it occurs: HYDROGEN BONDING WITHIN THE POLYPEPTIDE BACKBONE 22. Two types of secondary structure: ALPHA HELIX (“TWISTED”) AND BETA SHEET (FLAT AND FOLDED “ACCORDIAN”) 23. Four chemical interaction that occur in tertiary structure: SALT BRIDGES (ACID-BASE, IONIC BONDS); DISULFIDE BONDS (S-S); HYDROGEN BONDING (EXAMPLE: N-H-O; MUST HAVE TWO ELECTRONEGATIVE ATOMS); AND NON POLAR HYDROPHOBIC (WATER FEARING, TWISTS AWAY FROM WATER) 24. Two types quaternary structure: FIBROUS (LONG, STRINGY); AND GLOBULAR (LIKE A BLOB) 25. Compare tertiary and quaternary structure: TERTIARY STRUCTURE INVOVLES ONLY ONE POLYPEPTIDE CHAIN; QUATERNARY STRUCTURE IS WHEN TWO POLYPEPTIDE CHAINS INTERACT CLASSIFICATION and FOOD SOURCES 26. What makes a protein complete? A PROTEIN IS COMPLETE IF IT CONTAINS ALL OF THE ESSENTIAL AMINO ACIDS 27. What are food sources of complete proteins? ANIMAL PRODUCTS; MEAT, MILK 28. What makes a protein incomplete? A PROTEIN IS INCOMPLETE IF IT DOES NOT CONTAIN ALL OF THE ESSENTIAL AMINO ACIDS 29. List food sources of incomplete proteins. VEGETABLES PROTEIN FUNCTION 30. What is the relationship between structure and function? STRUCTURE DETERMINES FUNCTION 31. Can proteins provide energy? YES, 4 KCALS/GRAM 32. Explain why proteins are generally not used as a source of energy. PROTEINS HAVE SO MANY VARIOUS VITAL ROLES THAT IT IS NOT FAVORABLE TO USE THEM FOR ENERGY 33. How do proteins protect you from illness? SOME PROTEINS FUNCTION AS ANTIBODIES, WHICH “MARK” FOREIGN INVADERS (BACTERIA, VIRUSES) FOR DESTRUCTION 34. How are proteins involved in letting your body know what to do and when to do it? SOME PROTEINS ARE HORMONES; HORMONES SIGNAL ANOTHER PART OF YOUR BODY TO DO SOMETHING, MAKE SOMETHING, ETC. 35. How are proteins involved in, for example, getting oxygen to your cells? SOME PROTEINS FUCTION AS TRANSPORTERS AROUND YOUR BODY (LIKE HEMOGLOBIN DELIVERING OXYGEN TO YOUR CELLS); SOME PROTEINS FUNCTION AS TRANSPORTERS FROM THE OUTSIDE OF A CELL OR MEMBRANE TO THE INSIDE OF A CELL OR MEMBRANE (LIKE ATP SYNTHASE LETTING H+ IONS THROUGH THE MEMBRANE DURING CHEMIOSMOSIS) 2 36. How are proteins involved in the acid-base balance of your body? SOME PROTEINS ACT AS BUFFERS; HELP BODY RESIST CHANGE IN PHIF TOO ACIDIC, “TAKE UP” H+; IF TOO BASIC, RELEASE H+ 37. How are proteins involved in the fluid balance of your body? VERY SIMPLY, BECAUSE OF THE PRESENCE OF CERTAIN PROTEINS IN THE BLOOD, FLUID MOVES BACK FROM TISSUES INTO THE BLOODSTREAM; WITHOUT THESE PROTEINS, FLUID BUILDS UP INSIDE TISSUES, AND THE TISSUE SWELLS 38. What structural role do proteins fulfill? PROTEINS FORM HAIR, NAILS, MUSCLES, TENDONS AND LIGAMENTS 39. FIBROUS: LONG, THIN, ABLE TO CONTRACT MUSCLE; GLOBULAR: MOVE THROUGH BLOODSTREAM, CARRY THINGSHEMOGLOBIN (GLOBULAR) FUNCTION: ENZYMES 40. Define enzyme. SPECIALIZED PROTEINS THAT CATALYZE BIOCHEMICAL REACTIONS 41. Why is an enzyme’s shape so important? Explain the “lock and key” model. EACH ENZYME ONLY CATALYZES ONE SPECIFIC REACTION; FOR EXAMPLE CATALASE ONLY CATALYZES THE REACTION H202 H2O + O2; THE STRUCTURE OF THE ENZYME, CATALASE, MUST FIT THE STRUCTURE OF THE SUBSTRATE, H2O2, PERFECTLY OR THE REACTION CANNOT BE CATALYZED AND WILL NOT HAPPEN; THIS “FITTING” IS REFERRED TO AS THE LOCK AND KEY (ENZYME-SUBSTRATE COMPLEX); THIS EMPHASIZES THE IMPORTANT OF STRUCTURE = FUNCTION 42. Explain what happens to this enzyme’s activity at 55 degrees AND WHY: THE ENZYME STOPS WORKING BECAUSE IT IS TOO FAR AWAY FROM ITS OPTIMUM TEMPERATURE OF 40; IT MAY BE DENATURED, WHICH MEANS ITS SHAPE HAS BEEN CHANGED; SINCE ENZYME FUNCTION ON STRUCTURE, IF ITS SHAPE IS CHANGED, IT CAN’T FUNCTION 43. What will happen to the rate of an enzyme reaction as it is heated from very cold (near freezing) to very hot (boiling)? b. it will increase, then decrease, then be zero 44. At which pH do enzymes function best? e. The optimal pH depends on the particular enzyme CATALASE LAB 45. What effect do extreme environments have on the functionality of enzymes? What is this the direct result of? Extreme environments disrupts bonding and the enzyme loses structure. 3