Amino Acids Structure and Properties
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Questions and Answers

Which of the following is true about proteins?

  • All proteins are polymers of 300 amino acids.
  • Proteins are composed of a number of amino acids linked by ester bonds.
  • Proteins are not important for biological systems.
  • Most proteins are composed of alpha amino acids. (correct)
  • How many amino acids are seen in the human body?

  • 300
  • 100
  • 50
  • 20 (correct)
  • What type of amino acid contains no ring structure?

  • Aromatic amino acids
  • Aliphatic amino acids (correct)
  • Basic amino acids
  • Acidic amino acids
  • Which group is attached to the same carbon atom in alpha amino acids?

    <p>Amino group and carboxyl group</p> Signup and view all the answers

    What type of bonds link amino acids in proteins?

    <p>Peptide bonds</p> Signup and view all the answers

    Which protein is responsible for muscle contraction?

    <p>Collagen protein</p> Signup and view all the answers

    How many different classifications of amino acids are mentioned based on their structure?

    <p>1</p> Signup and view all the answers

    Which type of amino acid contains a ring structure?

    <p>Aromatic amino acids</p> Signup and view all the answers

    What is the composition of proteins?

    <p>Amino acids linked by peptide bonds</p> Signup and view all the answers

    What is the significance of alpha amino acids?

    <p>They are the primary building blocks of proteins.</p> Signup and view all the answers

    Which type of protein is essential for bone structure?

    <p>Collagen protein</p> Signup and view all the answers

    What type of bonds attach the amino and carboxyl groups in alpha amino acids?

    <p>Peptide bonds</p> Signup and view all the answers

    Which type of proteins contain colored prosthetic groups?

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

    What is the function of amino acid derivative T4?

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

    Which proteins contain metal ions?

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

    What is the characteristic of Phosphoproteins?

    <p>Contain phosphorus</p> Signup and view all the answers

    Which amino acid gives histamine by decarboxylation?

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

    What is the prosthetic group in hemoglobin?

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

    Which type of proteins are examples of Phosphoproteins?

    <p>Casein and Vitellin</p> Signup and view all the answers

    What negatively charged component does DNA combine with?

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

    Which enzyme contains Zinc as a metal ion?

    <p>Carbonic anhydrase</p> Signup and view all the answers

    What is the function of some hormone polypeptides like TSH, LH, FSH, GH?

    <p>Hormone regulation</p> Signup and view all the answers

    Which protein example is NOT correctly matched with its type?

    <p>Flavoproteins - Chromoproteins</p> Signup and view all the answers

    Which protein carries a colored prosthetic group that is yellow in color?

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

    Which amino acid is classified as purely ketogenic?

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

    Which of the following amino acids is both partially ketogenic and partially glucogenic?

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

    Which amino acid is classified as essential and has a purely glucogenic metabolic fate?

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

    Which type of protein is responsible for muscle contraction?

    <p>Structural proteins</p> Signup and view all the answers

    Which type of protein contains a non-protein prosthetic group?

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

    Which amino acid derivative cannot be made by the body and is essential for normal growth?

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

    Which type of amino acid contains a ring structure and is hydrophobic in nature?

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

    Which amino acid contains both imine (NH) and carboxyl (COOH) functional groups?

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

    Which amino acid is classified as both partially glucogenic and partially ketogenic in humans?

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

    Which type of protein carries the plasma lipid?

    <p>Transport proteins</p> Signup and view all the answers

    Which amino acid derivative is predominantly ketogenic in humans?

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

    Study Notes

    • Lecture by Dr. Reyadh Hanifah at the College of Medicine, University of Al-Najaf, in the Department of Chemistry and Pharmacy, focusing on Amino Acids and Proteins.
    • Proteins are essential biological molecules responsible for major structural and functional aspects of the body.
    • All proteins are polymers of amino acids, linked by peptide bonds.
    • There are 20 essential amino acids present in the human body.
    • Amino acids can be classified based on their structure and side chains.
    • Structurally, amino acids can be classified into Aliphatic, Aromatic, and Heterocyclic, with further subcategories based on side chains.
    • Aliphatic amino acids include mono amino monocarboxylic acids and mono amino dicarboxylic acids.
    • Aromatic amino acids contain phenyl or phenol rings, such as Phenylalanine and Tyrosine.
    • Heterocyclic amino acids contain other types of rings, like Tryptophan and Histidine.
    • Imino acids, such as Proline, contain both imine (NH) and carboxyl (COOH) functional groups.
    • Amino acids can also be classified based on their side chains, which determine their hydrophobic or hydrophilic nature.
    • Nonpolar side chains include Ala, Val, Leu, Ile, and aromatic amino acids Methionine, Proline, Phe, and Trp.
    • Polar side chains can be uncharged (Gly, Ser, Thr, Cys, Tyr, Gln, and Asn) or charged (Asp, Glu, Lys, Arg, and His).
    • Amino acids can also be classified based on their metabolic fate.
    • Purely ketogenic amino acids, like Leucine and Lysine, are converted to ketone bodies.
    • Partially ketogenic and glucogenic amino acids, such as Isoleucine, Phe, Thr, and Tryptophan, enter both the ketogenic and glucogenic pathways.
    • Purely glucogenic amino acids, including all the remaining 13 amino acids, enter only into the glucogenic pathway.
    • Amino acids can also be classified based on their nutritional requirements.
    • Essential amino acids, like Iso, Leu, Thr, Val, Met, Phe, Trp, and Lys, cannot be produced by the body and must be obtained from food.
    • Partially essential or semi-essential amino acids, like His and Arg, are required for growth in children but not for adults.
    • Non-essential or dispensable amino acids, like the remaining 10 amino acids, can be synthesized by the body.
    • Proteins can be classified based on their function.
    • Catalytic proteins, such as enzymes, play a role in catalyzing biochemical reactions.
    • Structural proteins, like collagen and elastin, provide structure and support.
    • Contractile proteins, such as myosin and actin, facilitate muscle contraction.
    • Transport proteins, like hemoglobin, myoglobin, albumin, and transferrin, transport various substances within the body.
    • Regulatory proteins or hormones, such as ACTH, insulin, and growth hormone, regulate various physiological processes.
    • Genetic proteins, like histones, play a role in DNA packaging and organization.
    • Protective proteins, such as immunoglobulins and interferons, protect the body against pathogens and damage.
    • Proteins can also be classified based on composition and solubility.
    • Simple proteins, which only contain amino acids, can be further classified into Albumin and Globulins.
    • Albumin is soluble in water and coagulates by heat, with a molecular weight of 69,000.
    • Globulins are insoluble in pure water but soluble in dilute salt solutions and coagulate by heat, with examples including serum globulins.
    • Conjugated proteins consist of a protein combined with a non-protein part, called a prosthetic group.
    • Glycoproteins are proteins combined with carbohydrates, with hydroxyl groups of serine or threonine and amide groups of asparagine and glutamine forming linkages with carbohydrate residues.
    • Lipoproteins are proteins loosely combined with lipid components, occurring in blood and on cell membranes and in plasma.
    • Nucleoproteins are proteins attached to nucleic acids.
    • Chromoproteins contain colored prosthetic groups.
    • Phosphoproteins contain phosphorus.
    • Metalloproteins contain metal ions.
    • Amino acids have various functions in the body, including as components of body peptides and proteins, hormones, and amines.
    • Essential amino acids serve as building blocks for body peptides and proteins.
    • Some hormones are polypeptides or amino acid derivatives, such as TSH, LH, FSH, and T4.
    • Some amino acids, like histidine, can give amines by decarboxylation, such as histamine, which is a vasodilator.

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