Biochemistry: Protein Structures and Bonds
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Questions and Answers

What type of bond is formed between the α-amino and carboxyl groups of amino acids?

  • Ionic bond
  • Van der Waals force
  • Hydrogen bond
  • Peptide bond (correct)
  • What is the result of the reaction between Gly and Ala?

  • Polypeptide
  • Tripeptide
  • Dipeptide (correct)
  • Glycyl-alanine (correct)
  • Which type of interaction is characterized by the sharing of electrons?

  • Covalent bond (correct)
  • Hydrogen bond
  • Electrostatic interaction
  • Van der Waals force
  • What causes denaturation in proteins due to temperature changes?

    <p>Heat application (A)</p> Signup and view all the answers

    Which of the following describe the denaturation effect due to pH changes?

    <p>Alteration of ionization of charged side chains (D)</p> Signup and view all the answers

    What is an example of a denaturing agent used in laboratories to study proteins?

    <p>Sodium dodecyl sulfate (SDS) (C)</p> Signup and view all the answers

    Which type of interaction occurs at distances of 3-5 Å?

    <p>Van der Waals interactions (D)</p> Signup and view all the answers

    What is the energy range (in kcal/mol) associated with covalent bonds?

    <p>30-100 (D)</p> Signup and view all the answers

    Study Notes

    Peptide and Peptide Bonds

    • Amino acids are covalently linked forming an amide bond between the α-amino and carboxyl groups.
    • This bond is called a peptide bond.
    • The products formed from amino acid unions are called peptides.
    • Linking two amino acids creates a dipeptide (e.g., Gly-Ala).
    • This reaction is considered a simple elimination of a water molecule.

    Protein Structures and Interactions

    • Table of Protein Interactions
      • Type | Mechanism | Energy (kcal/mol) | Interaction Distance (Å) | Interacting groups
      • Covalent | Electron sharing | 30-100 | 1-2 | C-C, C-N, C=O, C-S, C-N-C
      • Electrostatic/Salt Bridges | Coulombic attraction between opposite charges | 10-20 | 2-3 | -NH3+, -COO-
      • Hydrogen Bonds | Shared hydrogen between electronegative atoms | 2-10 | 2-3 | -N-H···O=C-, -N-H···O-H
      • Van der Waals | Induced dipole moments in polar groups | 1-3 | 3-5 | Polar groups

    Protein Denaturation

    • Temperature Changes: Heat is a common denaturing agent used in food processing assisting in protein digestion. It also disables inhibitors.
    • pH Changes: A change in pH can lead to significant protein conformation modifications due to ionization changes in charged side chains and affect the amount of stabilizing salt bridges.
    • Detergents: Denaturing proteins with detergents, (e.g., SDS), is common in lab settings. Detergents' amphiphilic nature helps with this process.

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    Description

    Explore the fundamental concepts of peptide bonds, amino acid interactions, and protein structures in this biochemistry quiz. Understand the mechanisms and energy associated with various types of protein interactions, crucial for studying biological processes. Test your knowledge on the basics of protein formation and denaturation.

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