Protein Structure and Analysis Techniques Quiz
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Questions and Answers

What is the primary structure of a protein?

  • The 3D folded structure of the protein
  • The sequence of amino acids (correct)
  • The presence of disulfide bonds
  • The arrangement of multiple polypeptides

    • What is the consequence of a defect in the primary structure of a protein?

  • It changes the protein's 3D structure
  • It alters the arrangement of polypeptides
  • It affects the formation of disulfide bonds
  • It can lead to diseases (correct)

    • What is the significance of the N-terminal and C-terminal in a polypeptide chain?

  • They determine the direction of the sequence (correct)
  • They control the protein's enzymatic activity
  • They are responsible for protein denaturation
  • They form hydrogen bonds with other chains

    • What type of amino acid residues are rarely found in the alpha helix due to their structural properties?

    <p>Proline and glycine</p> Signup and view all the answers

    Which type of protein structure involves the 3-D arrangement of all atoms in a protein and contains the active site where reactions occur?

    <p>Tertiary structure</p> Signup and view all the answers

    What gives strength and hardness to α-keratin in structures like rhinoceros horn?

    <p>Disulphide bonds between coiled coils</p> Signup and view all the answers

    Which chemical sequencing process labels and removes the amino-terminal residue from a peptide, leaving all other peptides intact?

    <p>Edman's degradation</p> Signup and view all the answers

    What technique is used to determine protein sequences and elucidate the history of life on earth?

    <p>Tandem MS or MS/MS</p> Signup and view all the answers

    How is protein concentration commonly determined using UV spectrophotometry?

    <p>Using the Beer-Lambert equation</p> Signup and view all the answers

    What is the primary structure of collagen?

    <p>Left-handed triple helix with Gly-X-Y repeating tripeptide unit</p> Signup and view all the answers

    What causes denaturation of proteins?

    <p>Heat affecting H bonds</p> Signup and view all the answers

    What is the structure of myoglobin?

    <p>Backbone of 8 α helices with β turns</p> Signup and view all the answers

    What is the predominant conformation of silk fibroin?

    <p>Antiparallel β conformation rich in Ala and Gly residues</p> Signup and view all the answers

    What is the function of vitamin C in relation to collagen?

    <p>Stabilizes collagen structure</p> Signup and view all the answers

    What is the structure of hemoglobin?

    <p>4 polypeptide chains – 2α and 2β</p> Signup and view all the answers

    Collagen is a globular protein with a recognizable folding pattern involving two or more elements of secondary structure.

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

    Silk fibroin is predominantly in the β conformation, rich in Ala and Gly residues.

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

    Denaturation of proteins is caused by disruption of the hydrophobic aggregation of nonpolar amino acid side chains and hydrogen bonds.

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

    Myoglobin has a predominant antiparallel β conformation.

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

    Collagen fibrils are made up of collagen in a parallel fashion and cross-linked for strength.

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

    Explain the structure and composition of collagen fibrils at a molecular level, including the role of specific amino acid residues.

    <p>Collagen fibrils are supramolecular structures composed of a triple helix of collagen, with each collagen molecule consisting of three left-handed α chains. These α chains are rich in glycine (Gly), proline (Pro), and 4-hydroxyproline (4-Hyp), with a repeating tripeptide unit of Gly–X–Y, where X is often Pro and Y is often hydroxyproline (Hyp). The collagen fibrils are cross-linked by lysine (Lys) or histidine (His) residues, contributing to their strength and stability.</p> Signup and view all the answers

    Discuss the significance of ascorbic acid (vitamin C) in maintaining the stability of collagen and the implications of vitamin C deficiency.

    <p>Ascorbic acid (vitamin C) plays a crucial role in maintaining the stability of collagen by facilitating the post-translational modification of proline and lysine residues, which are essential for collagen maturation and cross-linking. A deficiency in vitamin C leads to the instability of collagen, resulting in the deterioration of connective tissues and diseases such as scurvy.</p> Signup and view all the answers

    Provide an overview of the tertiary and quaternary structure of myoglobin, emphasizing its unique features and functional significance.

    <p>Myoglobin is a globular protein with a tertiary structure consisting of a heme group coordinated within a hydrophobic pocket formed by a single polypeptide chain. This structure allows myoglobin to efficiently bind and store oxygen in muscle tissues. Additionally, myoglobin contains a backbone of eight α helices with β turns, and its quaternary structure involves a single polypeptide chain of 153 amino acid residues, contributing to its role in oxygen storage and muscle function.</p> Signup and view all the answers

    Study Notes

    Protein Structure and Analysis Techniques

    • Fredrick Sanger determined the amino acid sequence in bovine insulin in 1953.
    • Edman's degradation is a two-step chemical sequencing process that labels and removes the amino-terminal residue from a peptide, leaving all other peptides intact.
    • For larger proteins, disulfide bonds must be eliminated by performic acid or dithiothreitol (DTT).
    • Mass spectrometry provides an alternative method to determine amino acid sequences, offering accurate molecular weight and short sequence determination in a short time.
    • Two techniques developed to solve the problem of mass spectrometry not working for large macromolecules are MALDI MS and ESI MS.
    • Tandem MS or MS/MS is used to determine protein sequences and elucidate the history of life on earth.
    • Tracing evolution involves identifying suitable families of homologous proteins and using them to reconstruct evolutionary paths.
    • Aromatic R groups in amino acids have various properties, including UV light absorption at 280 nm for protein characterization.
    • Protein concentration can be determined using UV spectrophotometry and the Beer-Lambert equation.
    • The Bradford assay uses a standard calibration curve of bovine serum albumin (BSA) to determine protein concentration.
    • M1V1 = M2V2 equation is used to prepare stock solutions of protein standards.
    • The common protein secondary structures include α-helix, β conformations, β-turn, and random coil, with the α-helix being observed in hair and porcupine quills.

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    Description

    Test your knowledge of protein structure and analysis techniques with this quiz. Explore topics such as amino acid sequencing, mass spectrometry, evolution tracing, protein characterization, and concentration determination.

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