Proteins Quiz

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Questions and Answers

What type of bonds connect amino acids in a protein?

  • Peptide bonds (correct)
  • Ionic bonds
  • Hydrogen bonds
  • Disulfide bonds

What percentage of the dry weight of cells do proteins constitute?

  • 30%
  • 60%
  • 20%
  • 50% (correct)

What is unique about glycine among the 20 common amino acids?

  • It is the largest amino acid
  • It is the simplest amino acid (correct)
  • It is an imino acid
  • It is the only D-isomer

What is the term for the process by which amino acids are connected to form a protein?

<p>Protein synthesis (C)</p> Signup and view all the answers

What type of amino acids are the most common?

<p>α-amino acids (C)</p> Signup and view all the answers

What is the meaning of the Greek word 'proteios', from which the term 'protein' is derived?

<p>First of importance (B)</p> Signup and view all the answers

What is the characteristic feature of chiral carbon centers in amino acids?

<p>Attached to four different substituents (A)</p> Signup and view all the answers

What is the characteristic of L-amino acids found in the body?

<p>Amino group on the left (B)</p> Signup and view all the answers

What type of proteins are derived from simple or conjugated proteins through physical or chemical means?

<p>Derived proteins (D)</p> Signup and view all the answers

What is the primary difference between complete and incomplete proteins?

<p>Adequacy of essential amino acids (B)</p> Signup and view all the answers

What is the process called when peptide bonds are broken by treatment with aqueous acid, base, or certain enzymes?

<p>Protein hydrolysis (D)</p> Signup and view all the answers

What is the term for proteins that lack one or more essential amino acids in correct proportion?

<p>Incomplete proteins (B)</p> Signup and view all the answers

What is the effect of heat on protein structure?

<p>It cleaves hydrogen bonds (A)</p> Signup and view all the answers

What is the purpose of combining two or more incomplete proteins?

<p>To create a complete protein (C)</p> Signup and view all the answers

What is the primary structure of a protein that remains intact during denaturation?

<p>Primary structure (A)</p> Signup and view all the answers

What is the effect of reducing agents on protein structure?

<p>They break disulfide bonds (B)</p> Signup and view all the answers

What is the primary role of the amino acid leucine in the body?

<p>Maintenance of nitrogen balance and energy supply (D)</p> Signup and view all the answers

Which amino acid is involved in calcium absorption and tissue repair?

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

What is the term for the amino acid that is in shortest supply in relation to need?

<p>Limiting amino acid (D)</p> Signup and view all the answers

Which of the following amino acids has hepatoprotective properties?

<p>Methionine (C)</p> Signup and view all the answers

What is the primary function of proteins in the body?

<p>To provide structure and strength to cells and tissue (D)</p> Signup and view all the answers

Which of the following foods is a rich source of the limiting amino acid lysine?

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

What is the consequence of a shortage of a limiting amino acid?

<p>Decreased protein synthesis (B)</p> Signup and view all the answers

Which amino acid is involved in neuronal function and immunity?

<p>Tryptophan (B)</p> Signup and view all the answers

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Study Notes

Proteins

  • Complex organic macromolecules containing carbon, hydrogen, oxygen, nitrogen, and usually sulfur
  • Linear polymers of amino acids connected by peptide bonds
  • Diverse and abundant class of biomolecules, making up about 50% of the dry weight of cells
  • Not stored in the body, so they must be consumed daily

Amino Acids

  • Organic compounds containing an amino group (NH2) and a carboxylic acid group (COOH)
  • Building blocks of proteins
  • 20 common amino acids, with most being chiral molecules
  • Most amino acids are α-amino acids, and all amino acids in the body are L-isomers
  • Exceptions: Glycine (simplest amino acid, achiral) and Proline (imino acid)

Classification of Proteins

  • According to composition: derived proteins (e.g. denatured proteins and peptides)
  • According to nutritional basis:
    • Complete proteins: contain all essential amino acids in correct proportion (e.g. meat, fish, dairy, egg)
    • Incomplete proteins: lack one or more essential amino acids in correct proportion (e.g. grains, nuts, beans, seeds, peas, corn)
    • Complementary proteins: combining two or more incomplete proteins to create a complete protein

Properties of Proteins

  • Denaturation: loss of secondary, tertiary, and quaternary structures, but primary structure remains intact
  • Factors that cause protein denaturation: heat, detergents, acids and bases, salts, reducing agents, heavy metal ions, alcohol, and mechanical stress

Protein Hydrolysis

  • Breaking peptide bonds by treatment with aqueous acid, base, or certain enzymes
  • Primary structure of protein is cleaved by the addition of water
  • Involved in the development of antibodies and has important antiviral properties

Specific Amino Acids

  • Leucine: helps maintain nitrogen balance and energy supply, supports muscle building, and lowers cholesterol and LDL levels
  • Limiting amino acids: amino acids in shortest supply in relation to need, inhibits protein synthesis, and usually found in incomplete proteins

Examples of Limiting Amino Acids

  • Lysine: involved in growth, tissue repair, and collagen synthesis
  • Threonine: involved in lipid metabolism and intestinal health
  • Methionine: involved in detoxification, antioxidant functions, and liver health
  • Tryptophan: involved in neuronal function, immunity, and gut homeostasis

Functions of Proteins

  • Structure: provides strength to cells and tissue, chief constituents of skin, bones, hair, and nails
  • Other functions: enzymatic, transport, storage, and defense-related functions

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