Classification of Amino Acids
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Questions and Answers

Which elements are basic constituents of proteins?

  • Oxygen, Hydrogen, Carbon (correct)
  • Oxygen, Nitrogen, Calcium
  • Oxygen, Neon, Carbon
  • Helium, Hydrogen, Carbon

What type of bond links amino acids in proteins?

  • Peptide bond (correct)
  • Ionic bond
  • Covalent bond
  • Hydrogen bond

Proteins retain their biological activity within a limited range of which factors?

  • Temperature and pressure
  • pH and light intensity
  • pH and temperature (correct)
  • Pressure and light intensity

Which atom is found in the general structure of an amino acid and is labeled as the central α-carbon?

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

Which group forms part of the amino acid structure and is responsible for its acidic properties?

<p>Carboxyl group (D)</p> Signup and view all the answers

Which amino acid is classified as aliphatic?

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

How many amino acids are included in the aliphatic group mentioned?

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

Which code represents Lysine?

<p>Lys, K (D)</p> Signup and view all the answers

Which type of side chain do amino acids in the aliphatic group possess?

<p>Hydrocarbon side chains (B)</p> Signup and view all the answers

Which of the following is a basic amino acid?

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

How are amino acids differentiated from each other?

<p>By their side chain (C)</p> Signup and view all the answers

What type of chemical bond links the amino acids in peptides?

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

Which of the following hormones stimulates uterine contraction?

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

How much protein is destroyed daily during the continuous renewal process in the body?

<p>200 to 300 grams (D)</p> Signup and view all the answers

Which classification of proteins can be categorized based on their biological function?

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

What property of proteins is affected by pH levels?

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

What is the role of glutathione in the cell?

<p>Participates in Redox reactions (A)</p> Signup and view all the answers

Which amino acid is essential?

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

Which amino acid has an acidic side chain?

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

At what pH does an amino acid have no net charge?

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

Which amino acid is not essential?

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

What is the characteristic of amino acids that allows them to act as both acids and bases?

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

Which of the following amino acids are paired with their corresponding amides?

<p>Aspartic acid and Asparagine (A)</p> Signup and view all the answers

What type of bonds are involved in the quaternary structure of proteins?

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

Which type of protein structure determines the sequence of amino acids?

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

What is lost during the denaturation of a protein?

<p>Its secondary, tertiary, and quaternary structures (A)</p> Signup and view all the answers

Which of the following is a physical agent that can cause protein denaturation?

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

Which of the following proteins have a quaternary structure?

<p>Collagen, hemoglobin, keratin (A)</p> Signup and view all the answers

What structural level is described by the spatial arrangement of amino acids?

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

What effect does denaturation have on the physicochemical properties of proteins?

<p>It causes structural changes and loss of function (A)</p> Signup and view all the answers

Which is not a type of secondary structure of a protein?

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

What happens to the solubility of proteins when exposed to high concentrations of salts?

<p>It decreases. (A)</p> Signup and view all the answers

Which type of proteins include lipoproteins, glycoproteins, and metalloproteins?

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

Primary structure in proteins refers to the:

<p>sequence and identity of amino acids. (C)</p> Signup and view all the answers

Which type of interaction stabilizes the secondary structure of proteins?

<p>Hydrogen bonds. (C)</p> Signup and view all the answers

What effect does a low concentration of salts have on protein solubility?

<p>Increases solubility. (B)</p> Signup and view all the answers

Which is an example of a protein with secondary structure being alpha-helix?

<p>Miosin in muscles (B)</p> Signup and view all the answers

What is the normal recommended protein intake per day based on body weight?

<p>1.5 g per kg (A)</p> Signup and view all the answers

Which function is associated with hemoglobin and myoglobin?

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

What property allows proteins to maintain internal pH and osmotic balance?

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

Which of the following is NOT a property of proteins?

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

Which molecule is considered the 'building blocks' of proteins?

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

What type of bond is formed between two amino acids?

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

Flashcards

Proteins

Large, complex molecules made up of smaller building blocks called amino acids.

Amino acids

The building blocks of proteins, containing a central carbon atom, an amino group, a carboxyl group, a hydrogen atom, and a unique side chain.

Essential amino acids

Amino acids that cannot be synthesized by the human body and must be obtained from the diet.

Non-essential amino acids

Amino acids that can be synthesized by the human body from other molecules.

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Peptides

Chains of amino acids linked together by peptide bonds.

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Primary structure (of proteins)

The unique sequence of amino acids in a protein chain.

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Secondary structure (of proteins)

The local, three-dimensional arrangement of amino acids in a protein chain, often forming alpha-helices and beta-sheets.

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Tertiary structure (of proteins)

The overall three-dimensional shape of a protein, formed by interactions between its various amino acids.

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Quaternary structure (of proteins)

The arrangement of multiple polypeptide chains into a functional protein complex.

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Protein denaturation

The loss of a protein's native structure, often caused by changes in temperature, pH, or chemicals.

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Structural proteins

Proteins that provide structural support for cells and tissues.

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Enzymatic proteins

Proteins that catalyze biochemical reactions in cells.

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Hormonal proteins

Proteins that act as chemical messengers to regulate various bodily functions.

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Defensive proteins

Proteins that help defend the body against foreign invaders like bacteria and viruses.

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Transport proteins

Proteins that transport molecules across cell membranes and through the body.

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Homeostatic proteins

Proteins that help maintain the internal balance and stability of the body.

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Isoelectric point

The pH at which a protein has a net neutral charge.

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Solubility (of proteins)

The ability of a protein to dissolve in a solvent, often influenced by pH, salts, and temperature.

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Specificity (of proteins)

The ability of a protein to interact with specific molecules, often based on its shape and chemical properties.

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Polarizability (of proteins)

The tendency of a protein to be influenced by electrical charges, often impacting its interactions with other molecules.

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Flexibility (of proteins)

The ability of a protein to change its shape in response to its environment.

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Ability to form cross-links (of proteins)

The ability of proteins to form strong connections with other molecules, often influencing their structure and function.

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Solubility (of proteins)

The ability of a protein to dissolve in a solvent, which is influenced by factors such as pH, salt concentration, and the presence of non-polar solvents.

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Acid-base properties (of proteins)

The property of proteins related to their ability to act as acids or bases, which is determined by their isoelectric point.

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Oxytocin

A hormone that stimulates uterine contractions during labor and childbirth.

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Glucagon

A hormone that raises blood glucose levels by stimulating the release of glucose from the liver.

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Antibiotics

Substances that are used to kill or inhibit the growth of bacteria.

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Glutathione

A tripeptide that plays a crucial role in cellular redox reactions.

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Study Notes

Proteins

  • Biopolymers (macromolecules) composed of oxygen, hydrogen, carbon, sulfur, phosphorus, iodine, iron, and magnesium.
  • Preserve biological activity only within a relatively limited pH and temperature range.

Amino Acids

  • Building blocks of proteins
  • General formula: atomic hydrogen, alpha carbon, amino group, carboxyl group, and side chain
  • Classified based on their side chain:
    • Aliphatic (non-polar)
    • Basic (polar)
    • Acidic (polar)
  • Essential amino acids: cannot be synthesized by the human body and must be obtained through the diet
    • Phenylalanine
    • Histidine
    • Tryptophan
    • Threonine
    • Methionine
    • Valine
    • Lysine
    • Leucine
    • Isoleucine
  • Non-essential amino acids: can be synthesized by the human body
    • Alanine
    • Aspartic acid
    • Glutamic acid
    • Cysteine
    • Serine
    • Arginine
    • Tyrosine

Peptides

  • Linear chains of amino acids linked by amide bonds
  • Examples:
    • Oxytocin: hormone that stimulates uterine contraction
    • Glucagon: hormone that has actions opposite to insulin
    • Antibiotics
    • Glutathione: participates in cellular redox reactions

Protein Structure

  • Primary structure: sequence of amino acids in a protein
  • Secondary structure: spatial arrangement of amino acids in a protein (α-helix and β-pleated sheet)
  • Tertiary structure: 3D arrangement of the secondary structure
  • Quaternary structure: union of multiple polypeptide chains to form a complex protein
  • Denaturation: loss of native protein structure leading to loss of biological activity

Protein Functions

  • Structural: provide framework and support for cells and tissues
  • Enzymatic: catalyze chemical reactions
  • Hormonal: regulate various physiological processes
  • Defensive: create antibodies and regulate factors against foreign agents or infections
  • Transport: transport molecules and ions across cell membranes
  • Homeostatic: maintain pH and osmotic balance

Protein Properties

  • Acidity/basicity: isoelectric point
  • Solubility: affected by pH, salts, and non-polar solvents
  • Specificity
  • Polarizability
  • Flexibility
  • Ability to form cross-links
  • Solubility
  • Acid-base properties (isoelectric point)

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Description

This quiz covers the classification of amino acids based on their side chain, including aliphatic amino acids. Learn about the different types of amino acids and their characteristics.

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