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CBS: Protein Structure and Function
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CBS: Protein Structure and Function

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Questions and Answers

What is the main difference between the 20 universal structural amino acids?

  • Their R-group attached to the α-carbon (correct)
  • Their role in protein folding
  • Their molecular weight
  • Their ionization state at physiological pH
  • What is the functional importance of amino acid side chains?

  • They are involved in DNA replication
  • They define the properties and function of the amino acid (correct)
  • They are responsible for protein folding
  • They determine the molecular weight of the amino acid
  • What is the nature of the peptide bond between amino acids?

  • A covalent bond formed through the condensation of amino and carboxyl groups (correct)
  • A disulphide bond formed through oxidation
  • An ionic bond formed through electrostatic attraction
  • A non-covalent bond formed through hydrogen bonding
  • What is the role of hydrogen bonds in protein structure?

    <p>They are important for protein folding and stability</p> Signup and view all the answers

    What is the main structural feature of an α-helix?

    <p>A spiral staircase-like structure</p> Signup and view all the answers

    What is the result of defects in amino acid metabolism?

    <p>Disease</p> Signup and view all the answers

    What is the primary determinant of protein conformation?

    <p>The primary sequence of amino acids</p> Signup and view all the answers

    What is the nature of most folded proteins?

    <p>They are marginally stable</p> Signup and view all the answers

    What is the main difference between selenocysteine and cysteine?

    <p>The presence of Se instead of S</p> Signup and view all the answers

    What is the role of hydroxyproline in collagen?

    <p>It allows the formation of a triple helix structure</p> Signup and view all the answers

    What is the result of a defective phenylalanine hydroxylase enzyme?

    <p>Reduced production of tyrosine and hormones derived from it</p> Signup and view all the answers

    What is the characteristic of the peptide bond that allows for the formation of hydrogen bonds?

    <p>It has a partial negative charge on the oxygen atom and a partial positive charge on the nitrogen atom</p> Signup and view all the answers

    What is the role of enzymes in the formation of polypeptides?

    <p>They facilitate the formation of peptide bonds between amino acids</p> Signup and view all the answers

    What is the characteristic of the peptide bond that makes it resistant to rotation?

    <p>It is shorter than the standard C-N bond length</p> Signup and view all the answers

    What is the result of a defective tyrosinase enzyme?

    <p>Albinism</p> Signup and view all the answers

    What is the role of homocysteine in the synthesis of cysteine?

    <p>It is necessary for the synthesis of cysteine</p> Signup and view all the answers

    Study Notes

    Amino Acids

    • Amino acids have an amino group (-NH2) and a carboxylic group (-COOH) attached to the same carbon (α-carbon)
    • There are 20 universal structural amino acids encoded in DNA
    • Each amino acid has a unique R-group attached to the α-carbon, which defines its properties and function
    • At physiological pH, the amino and carboxyl groups are ionized

    Essential and Non-Universal Amino Acids

    • Some amino acids are essential for the human diet due to the lack of enzymes to synthesize them de novo
    • Other amino acids, such as hydroxyproline, selenocysteine, and homocysteine, exist in cells but are not universally encoded in DNA

    Peptide Bond

    • Amino acids polymerize to form polypeptides (proteins) via the formation of peptide bonds between the alpha amino and alpha carboxylic groups of adjacent amino acids
    • The peptide bond is very strong and has some features of a double bond:
      • It is shorter than the standard C-N bond length
      • There is no rotation
      • The R-groups are in the trans configuration
      • There is a partial negative charge on the oxygen atom and a partial positive charge on the nitrogen atom
    • These partial charges are important in the formation of hydrogen bonds that are key for protein structure

    Defects in Amino Acid Metabolism

    • Defects in metabolism result in a number of clinical conditions, such as:
      • Phenylketonuria (PKU), due to defective phenylalanine hydroxylase
      • Albinism, due to defective tyrosinase (tyr → melanin)

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    Description

    This quiz covers the structures of 20 common amino acids, their functional importance, and the nature of peptide bonds. It also explores the main structural features of an α-helix and its role in typical globular and membrane proteins.

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