Proteins and Amino Acids

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Questions and Answers

Which of the following is the term for the process that removes water to join monomers, forming polypeptides, oligopeptides, or dipeptides?

  • Translation
  • Hydrolysis
  • Dehydration synthesis (correct)
  • Replication

If a protein is found to be non-functional due to a significant change in its environment, such as extreme pH or temperature, which level of protein structure is most likely to be initially affected?

  • Tertiary (correct)
  • The change would impact all levels equally
  • Secondary
  • Primary

What characteristic defines amino acids as either hydrophobic or hydrophilic?

  • The number of peptide bonds they form.
  • The properties of their R-side group. (correct)
  • The presence or absence of a central carbon atom.
  • Their reaction to changes in pH.

If the optimal pH for pepsin is 1.5 and the optimal pH for salivary amylase is 6.3, how would placing both enzymes in a solution with a pH of 9 affect their function?

<p>Neither enzyme would function optimally. (C)</p> Signup and view all the answers

Enzymes increase the rate of reactions by:

<p>Decreasing the activation energy (D)</p> Signup and view all the answers

Which type of bond is directly responsible for the primary structure of a protein?

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

What kind of bonds are disrupted by changes in pH or temperature?

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

Given the optimal temperatures for Pectinase, Xylanase, and Cellulase are all around 45-51°C, what affect would a prolonged winter and average temperature of 15°C have?

<p>It would lower function by affecting the enzyme's primary &amp; tertiary structure. (B)</p> Signup and view all the answers

If a disease prevents disulfide bridges from forming correctly, which level of protein structure would be most directly affected?

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

If two amino acids are joined together, what is the resulting molecule called?

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

Flashcards

Amino acid

The smallest unit of a protein.

Peptide bond

A bond that connects two amino acids together.

Oligo-peptide

A chain of 3-10 amino acids.

Polypeptide

A chain of more than 10 amino acids.

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Hydrophobic amino acids

Water fearing, nonpolar amino acids.

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Hydrophilic amino acids

Water loving, polar amino acids.

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Dehydration synthesis

The process of removing water to form a bond.

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Catalyst

A substance that speeds up biological processes

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Active site

The location on an enzyme where the substrate binds.

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Low temperature

Affects the enzyme. Primary & tertiary structure will denature (change the shape)

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Study Notes

  • The shape of a molecule determines its role in cellular processes like metabolism, homeostasis, growth, development, and heredity.
  • Most cellular processes involve proteins acting as enzymes.

Proteins

  • The smallest unit of a protein is called an amino acid.
  • There are four parts to an amino acid bonded to a central carbon:
    • amine group
    • R-side group
    • Carboxyl group
    • Hydrogen

Protein Functions

  • Proteins are used for making other proteins, which make up enzymes
  • Proteins are used for several biological functions
  • Proteins transmit and express hereditary features.

Peptide bonds

  • Two amino acids together are connected by a peptide bond, forming a dipeptide.
  • 3-10 amino acids together form oligo-peptides.
  • More than 10 amino acids together form polypeptides.

Amino acids

  • Hydrophobic amino acids are nonpolar and repel water.
  • Hydrophilic amino acids are polar and interact with water.

Dehydration synthesis

  • Dehydration synthesis / condensation reaction is the process that removes water to create polypeptides/oligopeptides/dipeptides.
  • Proteins are made of carbon, hydrogen, oxygen, nitrogen, and sulfur.

Types of Bonds Review

  • Peptide bonds are covalent and strong, characterized by water removal from amine and carboxyl groups.
  • Hydrogen bonds are weak and characterized by hydroxyl groups.
  • Disulfide bonds are covalent and strong, characterized by two cysteines (S-S).
  • Salt bridges are ionic and medium in strength, characterized by positive and negative amino acid attractions.

Protein Structure

  • Primary structures are straight-chain, disrupted by peptide bonds, pH, and temperature
  • Secondary structures are alpha helix/beta sheets, bonded by H-bonds, disrupted by ethanol/polar solvents.
  • Tertiary structures are globular with full function, disulfide, salt bridges, disrupted by pH and temperature.
  • Quaternary structures are globular, with many tertiary structures, bonded by H-bonds, disrupted by ethanol/polar solvents.

Enzymes

  • Enzymes are catalysts, which speed up biological processes.
  • In an enzyme diagram:
    • The substrate binds slightly as the enzyme changes shape
    • The active site is where the substrate binds
    • The enzyme is the catalyst
  • When relating potential energy to a diagram
    • Products come after reactants
    • Activation energy without the enzyme is higher than with the enzyme

Additional notes from work sheets

  • The likely optimal temperature for Pectinase is 49-51°C
  • The likely optimal temperature for Xylanase is 49-51°C
  • The likely optimal temperature for Cellulase is 46-47°C
  • The optimal pH for pepsin is 1.5.
  • The optimal pH for salivary amylase is 6.3.
  • The optimal pH for alkaline phosphatase is 9.

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