39. How many different amino acids are used in making proteins? A 5 B. 10 C 15 D. 20 a 40. A denatured protein refers to

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39. How many different amino acids are used in making proteins? A 5 B. 10 C 15 D. 20 a 40. A denatured protein refers to

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39 How Many Different Amino Acids Are Used In Making Proteins A 5 B 10 C 15 D 20 A 40 A Denatured Protein Refers To 1
39 How Many Different Amino Acids Are Used In Making Proteins A 5 B 10 C 15 D 20 A 40 A Denatured Protein Refers To 1 (64.17 KiB) Viewed 37 times
39. How many different amino acids are used in making proteins? A 5 B. 10 C 15 D. 20 a 40. A denatured protein refers to a protein that is what? A Broken down into small pieces B. Broken down into individual amino acids C Unfolded but still maintains activity and function D. Unfolded with loss of activity and function 41. A family of proteins refers to what? A The same protein that functions in different ways B. Proteins that share a similar but non-Identical shape but have different functions C Proteins that share a similar but non-Identical shape that serve similar functions D. Proteins that originate from the same gene E. Proteins that are an identical shape but serve different functions 42. Phosphorylating a protein can act like a molecular switch and turn on or off a protein's activity. Adding a phosphate group to the protein is done by what family of enzymes? A Phosphatases B. Helicases C Kinases D. Chaperones E Proteosomes 43. Which type of proteins help misfolded proteins fold back into their proper shape? A Phosphatases B. Helicases C Kinases D. Chaperones E Proteosomes 44. Where on an amino add does phosphorylation take place? A Alpha-carbon B. Amino group C Carboxyl group D. Hydroxyl group E. Methyl group 45. What is Km of an enzyme reaction? A the madmum rate of the reaction B. the rate of the reaction with half as much enzyme C the concentration of substrate where the reaction rate is half maximal D. the concentration of Inhibitor required to reduce the reaction rate by half E the concentration of enzyme needed to saturate the substrate 46. How does a competitive inhibitor affect the typical graph of reaction rate versus substrate concentration in an enzyme saturation experiment? A Reduces both Km and Vmax B. Reduces Km but leaves Vmax unchanged C Increases Km and leaves Vmax unchanged D. km is unchanged but Vmax is reduced E. Both Km and Vmax are unchanged
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