Proteins and Amino Acids Overview

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Questions and Answers

What is the isoelectric point (pI) for glycine?

  • 9.60
  • 12.00
  • 5.97 (correct)
  • 2.34

During the first stage of glycine titration, which group loses its proton?

  • R group
  • —NH3+ group
  • —H2N group
  • —COOH group (correct)

What happens at the midpoint of the first titration stage of glycine?

  • All protons are removed.
  • Only the R group is deprotonated.
  • The solution becomes strongly alkaline.
  • pH equals the pKa of the deprotonating group. (correct)

How many buffering zones are present for one amino acid?

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

In the second stage of glycine titration, from which group is a proton removed?

<p>—NH3+ group (B)</p> Signup and view all the answers

What is the pKa value for the —COOH group of glycine?

<p>2.34 (C)</p> Signup and view all the answers

What characterizes the zwitterionic form of glycine?

<p>It has a net charge of zero. (A)</p> Signup and view all the answers

How is the pI of amino acids with charged R groups determined?

<p>By considering the arithmetic mean of deprotonation stages. (D)</p> Signup and view all the answers

What is the primary structure of a protein?

<p>The sequence of amino acids in a protein (A)</p> Signup and view all the answers

Which of the following amino acids is classified as nonpolar and aliphatic?

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

What is the role of enzymes in cellular reactions?

<p>To catalyze almost all cellular reactions (A)</p> Signup and view all the answers

How are amino acids structurally joined together in proteins?

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

Which amino acid is positively charged?

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

What distinguishes the various types of amino acids?

<p>Their side chain or R-group properties (A)</p> Signup and view all the answers

Which of the following statements about amino acids is incorrect?

<p>Every amino acid has the same structure. (D)</p> Signup and view all the answers

What is the significance of amino acids being referred to as the 'alphabet' of protein structure?

<p>They can be arranged in numerous combinations. (B)</p> Signup and view all the answers

Flashcards

Amino Acids

The building blocks of proteins, with 20 different types.

Peptide Bond

The covalent bond that links amino acids together in a protein chain.

Protein Primary Structure

The linear sequence of amino acids in a protein.

Enzyme

A protein that speeds up chemical reactions in a cell.

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Nonpolar Aliphatic R-group

Amino acid side chains that are hydrophobic (water-fearing).

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Polar Uncharged R-group

Amino acid side chains that are hydrophilic (water-loving).

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Charged R-groups

Amino acid side chains with positive or negative charges.

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Aromatic R-groups

Amino acid side chains containing a ring structure with delocalized electrons.

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Amino Acid Properties

Amino acids can act as both acids and bases, donating or accepting protons (H+).

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Amphoteric Nature

Amino acids possess both acidic and basic properties.

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Isoelectric Point (pI)

The pH at which an amino acid has a net zero electric charge, existing as a zwitterion.

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Titration Curve of Amino Acid

Graph showing the change in pH of a solution as an amino acid is titrated with a strong base.

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pKa Value

The pH at which half of the ionizable group is protonated/deprotonated.

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Zwitterionic Form

The specific form of an amino acid where both a positive and negative charge occur.

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Amino Acid Classification

Amino acids can be classified based on the properties of their side chain (R group).

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Charged R-groups De-protonation

Deprotonation of the R group occurs in stages, affecting the amino acid's electrical charge and thus the sequence of deprotonation.

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Study Notes

Proteins and Amino Acids

  • Proteins are composed of 20 different amino acids joined in various combinations and sequences.
  • This allows for a vast array of protein types with diverse functions, including enzymes, hormones, antibodies, transporters, and structural components like muscle fibers, feathers, and spider webs.
  • Enzymes are highly specialized catalysts for almost all cellular reactions, making them crucial for understanding life's chemistry.
  • Amino acids are the building blocks of proteins, like letters forming words.
  • Amino acids have characteristic side chains with unique chemical properties, which determines their role in protein function.
  • Amino acids bond together through peptide bonds, forming a linear sequence called the primary structure.

Amino Acid Classification

  • Amino acids are categorized by their side chain (R-group) properties.
  • Nonpolar, aliphatic: Glycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine
  • Polar, uncharged: Serine, Threonine, Cysteine, Asparagine, Glutamine
  • Positively charged: Lysine, Arginine, Histidine
  • Negatively charged: Aspartate, Glutamate
  • Aromatic: Phenylalanine, Tyrosine, Tryptophan

Amino Acid Properties

  • Amino acids are amphoteric, meaning they can act as both acids and bases.
  • They can donate or accept protons (H+).
  • The ability to donate a proton correlates to the acidity and affects the pH(pK).
  • The titration curve of an amino acid reveals critical information.

Titration Curve and pI

  • The titration curve plots pH against the amount of added base, providing important information about the pKa values of the amino acid's ionizing groups.
  • pKa values indicate the pH at which half of the amino acid molecules are deprotonated.
  • The isoelectric point (pI) is the pH where the amino acid carries a net zero charge, existing primarily as a zwitterion.
  • For amino acids without ionizable R-groups, the pI is the arithmetic mean of the pKa values of the acidic and basic groups.
  • Amino acids with charged R-groups have a more complex titration curve with three distinct stages.

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