Amino Acid Structure Quiz

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Questions and Answers

What structure is Alanine?

Alanine structure

What structure is Valine?

Valine structure

What structure is Isoleucine?

Isoleucine structure

What structure is Leucine?

<p>Leucine structure</p> Signup and view all the answers

What structure is Methionine?

<p>Methionine structure</p> Signup and view all the answers

What structure is Tyrosine?

<p>Tyrosine structure</p> Signup and view all the answers

What structure is Tryptophan?

<p>Tryptophan structure</p> Signup and view all the answers

What structure is Phenylalanine?

<p>Phenylalanine structure</p> Signup and view all the answers

What structure is Aspartate?

<p>Aspartate structure</p> Signup and view all the answers

What structure is Glutamate?

<p>Glutamate structure</p> Signup and view all the answers

What two amino acids are acidic?

<p>Aspartate, Glutamate</p> Signup and view all the answers

What structure is Lysine?

<p>Lysine structure</p> Signup and view all the answers

What structure is Arginine?

<p>Arginine structure</p> Signup and view all the answers

What structure is Histidine?

<p>Histidine structure</p> Signup and view all the answers

What three amino acids are basic?

<p>Lysine, Arginine, Histidine</p> Signup and view all the answers

What two amino acids are polar, not charged, and have hydroxyl groups?

<p>Serine, Threonine</p> Signup and view all the answers

What two amino acids are polar, not charged, and have carboxyamide groups?

<p>Asparagine, Glutamine</p> Signup and view all the answers

What structure is Serine?

<p>Serine structure</p> Signup and view all the answers

What structure is Threonine?

<p>Threonine structure</p> Signup and view all the answers

What structure is Asparagine?

<p>Asparagine structure</p> Signup and view all the answers

What structure is Glutamine?

<p>Glutamine structure</p> Signup and view all the answers

What structure is Cysteine?

<p>Cysteine structure</p> Signup and view all the answers

What amino acid has disulfide bonds and is mostly found in extracellular proteins?

<p>Cysteine</p> Signup and view all the answers

What structure is Glycine?

<p>Glycine structure</p> Signup and view all the answers

What amino acid can fit in tight places?

<p>Glycine</p> Signup and view all the answers

What structure is Proline?

<p>Proline structure</p> Signup and view all the answers

What is the imino acid?

<p>Proline</p> Signup and view all the answers

What four amino acids are polar with uncharged R groups?

<p>Serine, Threonine, Asparagine, Glutamine</p> Signup and view all the answers

Histidine can shift between positively charged and not charged depending on what?

<p>Local environment</p> Signup and view all the answers

Hydrophobic amino acids tend to be located where in proteins?

<p>Inside</p> Signup and view all the answers

Acidic amino acids have R groups that are what charge?

<p>Negatively</p> Signup and view all the answers

Basic amino acids have R groups that are what charge?

<p>Positively</p> Signup and view all the answers

What are the nine nonpolar hydrophobic amino acids?

<p>Glycine, Alanine, Leucine, Isoleucine, Valine, Proline, Tryptophan, Phenylalanine, Methionine</p> Signup and view all the answers

What are the six polar hydrophilic amino acids?

<p>Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine</p> Signup and view all the answers

Are the basic and acidic amino acids considered hydrophilic?

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

What hydrophobic amino acid is the exception and could interact with water?

<p>Tyrosine</p> Signup and view all the answers

Flashcards

Alanine

A nonpolar, aliphatic amino acid.

Valine

A nonpolar, branched-chain amino acid, hydrophobic.

Isoleucine

Nonpolar, branched-chain amino acid with hydrophobic properties.

Leucine

Nonpolar, branched-chain amino acid crucial for protein synthesis.

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Methionine

Contains a sulfur atom, nonpolar, initiates protein synthesis.

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Tyrosine

Polar, can engage in hydrogen bonding; derived from phenylalanine.

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Tryptophan

Nonpolar, precursors to serotonin, has aromatic structure.

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Phenylalanine

Has aromatic properties and is nonpolar; needed for synthesizing tyrosine.

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Aspartate

Acidic, negatively charged side chain; involved in metabolic pathways.

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Glutamate

Acidic, important neurotransmitter in the brain, negatively charged.

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Acidic Amino Acids

Known for their negatively charged R groups at neutral pH.

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Lysine

Basic, positively charged side chain; involved in protein interaction.

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Arginine

Basic, can donate protons; involved in metabolic functions.

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Histidine

Basic, can switch between charged and uncharged states, vital for enzyme activity.

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Serine

Polar, contains hydroxyl group; contributes to hydrogen bonds.

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Threonine

Similar to serine, has a hydroxyl group; polar and hydrophilic.

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Asparagine

Polar, possesses a carboxyamide group; involved in hydrogen bonding.

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Glutamine

Similar to asparagine, polar with carboxyamide group; important for nitrogen transport.

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Cysteine

Contains a thiol group, can form disulfide bonds, stabilizing protein structure.

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Glycine

Simplest amino acid, fits into tight spaces within proteins due to its small size.

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Proline

Unique imino acid, introduces rigidity in protein structure; often found in turns.

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Hydrophobic Amino Acids

Tend to be buried inside proteins to avoid contact with water.

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Polar Amino Acids

Facilitate hydrogen bonding due to their polar side chains.

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Hydrophilic Amino Acids

Basic and acidic amino acids are considered hydrophilic due to their charge properties.

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Acidic Amino Acids

Exhibit negatively charged side chains at neutral pH.

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Basic Amino Acids

Feature positively charged side chains, crucial for interactions with negatively charged groups.

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Histidine's Charge

Unique ability to switch charge based on local pH; involved in enzyme catalysis and protein function.

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Tyrosine's Polarity

An aromatic amino acid that can interact with water due to its hydroxyl group.

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Nonpolar, Hydrophobic Amino Acids

Hydrophobic amino acids that tend to cluster together in the protein core.

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Polar Hydrophilic Amino Acids

Water-soluble amino acids with polar side chains capable of forming hydrogen bonds.

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Study Notes

Amino Acid Characteristics

  • Alanine: Nonpolar, aliphatic amino acid.
  • Valine: Nonpolar, branched-chain amino acid, hydrophobic.
  • Isoleucine: Nonpolar, branched-chain amino acid with hydrophobic properties.
  • Leucine: Nonpolar, branched-chain amino acid crucial for protein synthesis.
  • Methionine: Contains a sulfur atom, nonpolar, initiates protein synthesis.
  • Tyrosine: Polar, can engage in hydrogen bonding; derived from phenylalanine.
  • Tryptophan: Nonpolar, precursors to serotonin, has aromatic structure.
  • Phenylalanine: Aromatic, nonpolar; needed for synthesizing tyrosine.
  • Aspartate: Acidic, negatively charged side chain; involved in metabolic pathways.
  • Glutamate: Acidic, important neurotransmitter in the brain, negatively charged.
  • Acidic Amino Acids: Aspartate and Glutamate, known for their negatively charged R groups.
  • Lysine: Basic, positively charged side chain; involved in protein interaction.
  • Arginine: Basic, can donate protons; involved in metabolic functions.
  • Histidine: Basic, can switch between charged and uncharged states, vital for enzyme activity.

Polar Amino Acids

  • Serine: Polar, contains hydroxyl group; contributes to hydrogen bonds.
  • Threonine: Similar to serine, has a hydroxyl group; polar and hydrophilic.
  • Asparagine: Polar, possesses a carboxyamide group; involved in hydrogen bonding.
  • Glutamine: Similar to asparagine, polar with carboxyamide group; important for nitrogen transport.
  • Cysteine: Contains a thiol group, can form disulfide bonds, stabilizing protein structure.

Other Amino Acid Features

  • Glycine: Simplest amino acid, fits into tight spaces within proteins due to its small size.
  • Proline: Unique imino acid, introduces rigidity in protein structure; often found in turns.
  • Hydrophobic Amino Acids: Tend to be buried inside proteins to avoid contact with water (e.g., Glycine, Alanine, Methionine).
  • Polar Amino Acids: Include Serine, Threonine, Asparagine, Glutamine, and Cysteine; facilitate hydrogen bonding.

Charge Characteristics

  • Acidic Amino Acids: Exhibit negatively charged side chains.
  • Basic Amino Acids: Feature positively charged side chains, crucial for interactions with negatively charged groups.

Unique Properties

  • Histidine: Unique ability to switch charge based on local pH; involved in enzyme catalysis and protein function.
  • Tyrosine: Exceptionally hydrophobic amino acid that can still interact with water due to its hydroxyl group.

Common Groupings

  • Nonpolar Hydrophobic Amino Acids: Include Glycine, Alanine, Leucine, Isoleucine, Valine, Proline, Tryptophan, Phenylalanine, Methionine.
  • Polar Hydrophilic Amino Acids: Include Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine.

General Knowledge

  • Hydrophilic Amino Acids: Basic and acidic amino acids are considered hydrophilic due to their charge properties.

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