Podcast
Questions and Answers
What distinguishes α, β, and δ amino acids?
What distinguishes α, β, and δ amino acids?
Why do amino acids have optical activity?
Why do amino acids have optical activity?
Which statement is true regarding amino acids found in mammalian proteins?
Which statement is true regarding amino acids found in mammalian proteins?
Which group is found at the alpha carbon of amino acids?
Which group is found at the alpha carbon of amino acids?
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What unique property do amino acids exhibit due to being zwitterions?
What unique property do amino acids exhibit due to being zwitterions?
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Which of the following amino acids is classified as an imino acid?
Which of the following amino acids is classified as an imino acid?
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What is the significance of L- and D- amino acids in biological systems?
What is the significance of L- and D- amino acids in biological systems?
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What results from the modification of standard amino acids?
What results from the modification of standard amino acids?
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Which of the following amino acids is classified as an essential amino acid?
Which of the following amino acids is classified as an essential amino acid?
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What is the characteristic of complete proteins?
What is the characteristic of complete proteins?
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Which of the following amino acids is considered semi-essential?
Which of the following amino acids is considered semi-essential?
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How are amino acids generally grouped?
How are amino acids generally grouped?
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Which non-polar amino acid has a hydrogen atom as its R group?
Which non-polar amino acid has a hydrogen atom as its R group?
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What type of proteins are most vegetable proteins classified as?
What type of proteins are most vegetable proteins classified as?
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Which of the following amino acids is NOT an aromatic amino acid?
Which of the following amino acids is NOT an aromatic amino acid?
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Which amino acids are involved in hydrophobic interactions due to their hydrocarbon R groups?
Which amino acids are involved in hydrophobic interactions due to their hydrocarbon R groups?
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Which of the following amino acids is classified as basic?
Which of the following amino acids is classified as basic?
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What distinguishes essential amino acids from non-essential amino acids?
What distinguishes essential amino acids from non-essential amino acids?
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Which amino acid is known for functioning as a neurotransmitter?
Which amino acid is known for functioning as a neurotransmitter?
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What role does the -OH group in tyrosine play in proteins?
What role does the -OH group in tyrosine play in proteins?
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Which of the following amino acids is negatively charged at pH 7.0?
Which of the following amino acids is negatively charged at pH 7.0?
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Which of the following classifications includes both glucogenic and ketogenic amino acids?
Which of the following classifications includes both glucogenic and ketogenic amino acids?
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Which amino acid contains a sulfur atom in its side chain, contributing to hydrophilic interactions?
Which amino acid contains a sulfur atom in its side chain, contributing to hydrophilic interactions?
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Which amino acid belongs to the polar category?
Which amino acid belongs to the polar category?
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What is a primary source of essential amino acids?
What is a primary source of essential amino acids?
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What characteristic of proline affects its flexibility in protein structures?
What characteristic of proline affects its flexibility in protein structures?
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Which statement accurately describes electrically charged amino acids?
Which statement accurately describes electrically charged amino acids?
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Which of the following amino acids is NOT classified as an aromatic amino acid?
Which of the following amino acids is NOT classified as an aromatic amino acid?
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What is the significance of the side chain properties in amino acids?
What is the significance of the side chain properties in amino acids?
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Which amino acid is a dimer of cysteine?
Which amino acid is a dimer of cysteine?
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What is the pK value of the α-carboxylic group in amino acids typically in the range of?
What is the pK value of the α-carboxylic group in amino acids typically in the range of?
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At what point is an amino acid considered electrically neutral?
At what point is an amino acid considered electrically neutral?
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What occurs in solutions that are more basic than the isoelectric point for amino acids?
What occurs in solutions that are more basic than the isoelectric point for amino acids?
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Which of the following amino acids is polar and uncharged?
Which of the following amino acids is polar and uncharged?
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Which amino acid has a second carboxyl group that affects its acidic properties?
Which amino acid has a second carboxyl group that affects its acidic properties?
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What does the term 'zwitterion' refer to in relation to amino acids?
What does the term 'zwitterion' refer to in relation to amino acids?
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What happens at the pH of an amino acid's isoelectric point?
What happens at the pH of an amino acid's isoelectric point?
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Study Notes
Amino Acid Structure
- Amino acids are organic molecules containing both carboxyl and amino groups.
- Amino acids are the building blocks of proteins.
- They contain a carboxylic acid group and an amino group on the alpha (α) carbon.
- Amino acids differ in their properties due to differing side chains.
- Side chains are called R groups.
α-Carbon
- The alpha carbon is an asymmetrical carbon atom giving the amino acids optical activity.
Amino Acid Structure
- Amino acids can be characterized as α, β, or δ depending on the location of the amino group in the carbon chain.
- α amino acids are found on the carbon adjacent to the carboxyl group.
- β amino acids are found on the 2nd carbon from the carboxyl group.
- δ amino acids are found on the 3rd carbon from the carboxyl group.
Amino Acids
- 20 standard amino acids are present in mammalian proteins.
- All amino acids have amphoteric properties, meaning they can act as both an acid and a base.
- All amino acids except glycine have optical activity.
- Amino acids are dipolar, having both charges.
- The positive end is NH3+.
- The negatve end is COO-.
- Non-standard amino acids come from modifications of standard amino acids.
- Amino acids have Stereoisomers.
- All amino acids except glycine have chiral carbon (asymmetrical carbon atom).
- L-amino acids are natural amino acids found in protein.
- D-amino acids are found in antibiotics and plant and bacterial cell walls.
Proline
- Proline is an imino acid, meaning it has a secondary amino group.
Amino Acid Abbreviations
- Each amino acid has a three letter abbreviation and a one letter symbol.
- The three letter abbreviation is commonly the first three letters of the amino acid name.
- The one-letter symbol is typically the first letter of the amino acid name.
- When these abbreviations are confusing, alternative abbreviations are used.
Amino Acid Functions
- Amino acids are the building blocks of proteins.
- Some amino acids and their derivatives function as neurotransmitters and other regulators.
- Neurotransmitters and regulators include L-dopamine, epinephrine, thyroxine, and histamine.
Classification of Amino Acids
- Essential or Non-Essential
- Glucogenic, ketogenic, or Glucogenic & ketogenic
- Neutral, acidic, and basic
- According to the side chain properties
Essential & Non-Essential Amino Acids
- Essential amino acids are not synthesized by the human body and must be obtained from the diet.
- Essential amino acids are present in dairy products.
- Sources of protein come from both animal and vegetable sources.
- Animal sources are complete proteins, meaning they contain all essential amino acids.
- Vegetable sources usually lack some essential amino acids.
- They are classified as semi-essential or conditionally essential amino acids, including arginine, cysteine, glutamine, glycine, and proline.
Essential Amino Acids
- Essential amino acids are: arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine.
- Non-Essential amino acids are: alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, tyrosine.
Complete Protein
- Complete protein contains all 10 essential amino acids.
- Incomplete protein lacks one or more essential amino acids.
- Most vegetable proteins are incomplete proteins with the exception of beans.
- Beans contain some complete protein.
Classification According to Side Chain Properties
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Non-polar (Hydrophobic)
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Side chain does not bind or give off protons.
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They promote hydrophobic interactions.
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They are clustered in the interior of a protein when in aqueous solution.
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They help give 3D shape to the protein structure.
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Non-polar (Hydrophobic), Aliphatic Amino Acids
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Glycine (Gly or G)
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Alanine (Ala or A)
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Valine (Val or V)
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Leucine (Leu or L)
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Isoleucine (Ile or I)
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Methionine (Met or M)
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Non-polar (Hydrophobic), Aromatic Amino Acids
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Phenylalanine (Phe or F)
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Tryptophan (Trp or W)
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Proline (Pro or P)
Polar (Hydrophilic) Uncharged Amino Acids
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Serine (Ser or S)
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Threonine (Thr or T)
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Cysteine (Cys or C)
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Tyrosine (Tyr or Y)
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Asparagine (Asn or N)
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Glutamine (Gln or Q)
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The six amino acids with polar, uncharged R groups are more hydrophilic due to the presence of hydroxyl groups, sulfur atoms, or amide groups.
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The SH group of two Cysteine residues in proteins can be oxidized to form a covalent disulfide bond.
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Cys often participates in hydrophobic interactions.
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Pro has a five-membered ring structure, being rigid in conformation and offering the least flexibility.
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Pro is often found in the bends of folded protein chains and on the surface of proteins.
Positively Charged (Basic) and Negatively Charged (Acidic) R Groups
- The most hydrophilic R groups are those either positively or negatively charged.
- Asp and Glu have a carboxyl group in their R groups.
- They have a net negative charge at pH 7.0.
- They are typically named aspartate and glutamate.
- Arg, Lys, and His have positively charged R groups at pH 7.0.
- Their R groups contain a guanidino, amino, or imidazole group respectively.
- The side chain of His can be positively or uncharged depending on the local environment near pH 7.0.
Polar (Hydrophilic) Charged Amino Acids
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Negatively charged
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Aspartic Acid (Asp or D)
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Glutamic Acid (Glu or E)
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Positively charged
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Lysine (Lys or K)
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Arginine (Arg or R)
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Histidine (His or H)
Cystine
- Cystine is a dimer of cysteine.
Sickle Cell Disease
- Sickle cell disease is a pathology that results from the substitution of polar glutamate by the non-polar valine in the B subunit of hemoglobin.
pK Value
- pK value measures the ability of an acid to donate a proton (dissociate).
- It is also known as pKa or the acid dissociation constant.
- pK value represents the pH at which 50% of the acid is dissociated.
- The pK values of α-carboxylic groups are typically in the range of 2.2.
- The pK values of α-amino groups are typically in the range of 9.4
- The smaller the pK value, the stronger the acid.
- The larger the pK values, the weaker the acid.
Zwitterion
- Zwitterion is a double ion.
- Zwitterion is formed when both NH3+ and COO- are ionized.
- At the isoelectric point (pI), the positive and negative charges in the zwitterion are equal.
- pI is the pH at which the molecule is electrically neutral.
Amino Acids as Acids or Bases
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Amino Acids as Acids
- In solutions that are more basic than the pI, the —NH3+ in the amino acid donates a proton.
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Amino Acids as Bases
- In solutions more acidic than the pI, the COO- in the amino acid accepts a proton.
pH and Ionization
- Acidic amino acids, such as aspartic acid, have a second carboxyl group that can donate and accept protons.
- The pI for aspartic acid occurs at a pH of 2.8.
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Description
This quiz explores the structure of amino acids, their classification based on the position of amino groups, and their role as building blocks of proteins. Test your knowledge about α, β, and δ amino acids, as well as their unique properties and functions in biological systems.