2BC3 Midterm
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Questions and Answers

Which of the following is correct about Edman degradation?

  • Treatment of protein at pH = 3 with PITC
  • Treatment with anhydrous acid results in cleavage of the C-terminal residue.
  • Edman degradation is required to determine the sequence of protein. (correct)
  • All of the above.
  • Which of the following statement is correct about fibrous proteins?

  • Fibrous proteins have 3º structure
  • Fibrous proteins are soluble
  • Fibrous proteins only have 2º structure (correct)
  • Fibrous proteins carry out metabolic functions
  • Which of the following statement is NOT correct about Loops?

  • Loops contribute to secondary structure
  • Loops can be quite long and “disordered”
  • Loops are held together by hydrogen bonding (correct)
  • Loops often contain hydrophilic residues
  • Which of the following is Globular protein?

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

    Which of the following is correct about β-Strands and β-Sheets?

    <p>All of the above</p> Signup and view all the answers

    The rise, pitch and the number of residues per turn of α-helix are

    <p>0.15 nm; 0.54 nm and 3.6</p> Signup and view all the answers

    In α-helix, C=O hydrogen-bonded to each ____ H-N on backbone

    <p>the 4th</p> Signup and view all the answers

    Which of the following chromatography should be used to separate proteins on the charge?

    <p>Ion exchange chromatography</p> Signup and view all the answers

    Which of the following interaction maintains the protein secondary structure?

    <p>hydrogen bonding</p> Signup and view all the answers

    Which of the following is correct about turns?

    <p>Turns consist of up to 5 residues that induce an abrupt change in direction</p> Signup and view all the answers

    What is the mobile phase for size exclusion chromatography?

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

    Which of the following residues is the most common in α-Helices?

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

    Which of the following is the subtype(s) of Mass spectrometry according to the ion source?

    <p>Both A and B</p> Signup and view all the answers

    SDS-PAGE is separating molecules according to_______.

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

    During size exclusion (gel filtration) chromatography, __________ proteins are eluted in the earlier fraction

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

    Which of the following statement is correct about domains?

    <p>Discrete, independently folded regions; typically perform a specific function</p> Signup and view all the answers

    Which of the following solution will disrupt the hydrogen bonding in tertiary structure?

    <p>all of the above</p> Signup and view all the answers

    Which of the following is correct about Lectin Affinity Chromatography?

    <p>All of the above</p> Signup and view all the answers

    Which of the following statement is correct about SDS-PAGE?

    <p>Denaturing gel electrophoresis using the detergent</p> Signup and view all the answers

    Study Notes

    Protein Structure and Chromatography

    • Edman degradation is a method to determine the N-terminal amino acid of a protein.
    • Fibrous proteins are composed of long, thin molecules and are often involved in structural or mechanical roles.
    • Loops are regions of protein structures that do not form α-helices or β-sheets and are often found on the surface of proteins.
    • Globular proteins are compact, roughly spherical molecules and are often involved in metabolic processes.

    Protein Secondary Structure

    • β-Strands are extended protein structures that are often found in β-sheets, which are composed of multiple β-strands held together by hydrogen bonds.
    • α-Helices are spiral-shaped protein structures that are stabilized by hydrogen bonds between the C=O and H-N groups of the backbone, with 3.6 amino acids per turn.

    Chromatography

    • Ion-exchange chromatography is used to separate proteins based on their charge.
    • Hydrogen bonds, ionic bonds, disulfide bonds, and hydrophobic interactions maintain protein secondary structure.
    • Size exclusion chromatography uses a mobile phase of buffer and separates molecules based on their size.

    Protein Analysis

    • Turns are a type of non-repetitive secondary structure and are often involved in protein-protein interactions.
    • Glutamic acid is the most common residue found in α-helices.
    • Matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) are subtypes of mass spectrometry.
    • SDS-PAGE separates molecules based on their size.

    Protein Interactions and Purification

    • Domains are independently folded regions of a protein that are often involved in specific functions.
    • Urea is a solution that can disrupt the hydrogen bonding in tertiary structure.
    • Lectin affinity chromatography is a type of affinity chromatography that uses lectins to purify proteins based on their carbohydrate content.
    • In size exclusion chromatography, larger proteins are eluted in the earlier fraction.

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    Description

    Quiz covering protein structure, including Edman degradation, fibrous and globular proteins, and protein secondary structures.

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