Biochemistry Chapter on Peptides and Proteins

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Questions and Answers

What is formed when two amino acids are covalently linked via a peptide bond?

  • Protein
  • Polypeptide
  • Peptide (correct)
  • Tripeptide

Which of the following best describes the mechanism of covalent bonds?

  • Hydrogen bonding
  • Mutual dipole induction
  • Electron sharing (correct)
  • Coulombic attraction

What change does applying heat to proteins typically cause?

  • Enhances enzyme activity
  • Facilitates protein digestion (correct)
  • Stabilizes protein structure
  • Increases protein synthesis

Which type of bond involves hydrogen being shared between molecules?

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

How does a change in physiological pH affect protein structure?

<p>It can lead to conformational changes. (C)</p> Signup and view all the answers

Which of the following is NOT a significant factor in the denaturation of proteins?

<p>Increased oxygen levels (D)</p> Signup and view all the answers

What interaction type is characterized by mutual dipole induction among non-polar groups?

<p>Van der Waals forces (C)</p> Signup and view all the answers

What is the energy range for covalent bonds according to their binding forces?

<p>30-100 kcal/mol (C)</p> Signup and view all the answers

Flashcards

Peptide Bond

A covalent bond formed between the α-amino group of one amino acid and the carboxyl group of another amino acid. The reaction involves the removal of a water molecule.

Primary Structure

The sequence of amino acids in a polypeptide chain. It is the most basic level of protein structure.

Protein Denaturation

The process of unfolding or disrupting the native conformation of a protein, leading to loss of its biological activity.

Detergent

Molecules that can disrupt protein structures by interacting with hydrophobic regions, leading to denaturation.

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Heat Denaturation

A type of denaturation caused by applying heat, often used in cooking to improve protein digestibility and deactivate harmful enzymes.

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pH Denaturation

Denaturation caused by changing the pH of a protein's environment, which disrupts electrostatic interactions that stabilize the protein's structure.

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Electrostatic Interaction

A chemical force responsible for interactions between charged groups, like the amino and carboxyl groups of amino acids.

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Hydrogen Bond

A weak interaction between a hydrogen atom covalently linked to an electronegative atom (like oxygen or nitrogen) and another electronegative atom.

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Study Notes

Peptide and Peptide Bonds

  • Amino acids link covalently, forming amide bonds (peptide bonds) between the α-amino and carboxyl groups.
  • Peptide bonds create peptides, and multiple peptides form proteins.
  • A dipeptide is formed when two amino acids join; an example is Gly-Ala.
  • Peptide bond formation is a simplified dehydration reaction producing a new molecule.

Protein Structure

3.5.2 Primary Structure

  • The primary structure is the first level of protein organization.

3.6.2 Denaturation by Temperature Changes

  • Heating is a common denaturing agent for proteins in food, aiding digestion and neutralizing enzyme inhibitors.

3.6.3 Denaturation by pH Changes

  • Changes in pH modify protein conformation through altered ionization of charged side chains.
  • This affects salt bridges, which are crucial for protein structure.

3.6.5 Denaturation by Detergents

  • Detergents like SDS are vital in protein studies for their denaturing abilities.
  • SDS works through amphiphilic properties.

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