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Questions and Answers
What is the primary element that distinguishes proteins from carbohydrates and lipids?
What is the primary element that distinguishes proteins from carbohydrates and lipids?
- Carbon
- Oxygen
- Hydrogen
- Nitrogen (correct)
Proteins are made up of more than 20 standard amino acids.
Proteins are made up of more than 20 standard amino acids.
False (B)
What are the small units that proteins can be broken down into called?
What are the small units that proteins can be broken down into called?
Amino acids
The Greek word that the term 'protein' is derived from means '______'.
The Greek word that the term 'protein' is derived from means '______'.
Match the following elements with their presence in proteins:
Match the following elements with their presence in proteins:
How many standard amino acids can proteins be composed of?
How many standard amino acids can proteins be composed of?
Who suggested the term 'proteins' to GJ Mulder?
Who suggested the term 'proteins' to GJ Mulder?
Which of the following amino acids is classified as having a non-polar R group?
Which of the following amino acids is classified as having a non-polar R group?
All amino acids with polar but uncharged R groups are hydrophobic.
All amino acids with polar but uncharged R groups are hydrophobic.
What is the one-letter symbol for Cysteine?
What is the one-letter symbol for Cysteine?
The amino acid ______________ has a positively charged R group.
The amino acid ______________ has a positively charged R group.
Match the amino acids with their classifications:
Match the amino acids with their classifications:
Which amino acid is commonly considered to have an ambiguous classification due to its side chain?
Which amino acid is commonly considered to have an ambiguous classification due to its side chain?
Glycine has the largest R group among amino acids.
Glycine has the largest R group among amino acids.
Name one amino acid that is classified as negatively charged.
Name one amino acid that is classified as negatively charged.
Out of the following amino acids, ______________ is classified as a polar but uncharged R group.
Out of the following amino acids, ______________ is classified as a polar but uncharged R group.
Which amino acid has both a polar side chain and an ionizable group?
Which amino acid has both a polar side chain and an ionizable group?
Which amino acid has a thiol ether side chain?
Which amino acid has a thiol ether side chain?
Proline is categorized as an a-amino acid.
Proline is categorized as an a-amino acid.
What is the formula for Tryptophan?
What is the formula for Tryptophan?
Tyrosine is a derivative of ___________ with a phenolic group.
Tyrosine is a derivative of ___________ with a phenolic group.
Match the following amino acids with their characteristics:
Match the following amino acids with their characteristics:
Which amino acid is known for its aromatic side chain?
Which amino acid is known for its aromatic side chain?
Valine is classified as a polar amino acid.
Valine is classified as a polar amino acid.
Which amino acid has an amide-bearing side chain?
Which amino acid has an amide-bearing side chain?
The amino acid ___________ features a side chain that can form hydrogen bonds due to its hydroxyl group.
The amino acid ___________ features a side chain that can form hydrogen bonds due to its hydroxyl group.
What distinguishes Proline from other amino acids?
What distinguishes Proline from other amino acids?
Which of the following amino acids is classified as a dicarboxylic amino acid?
Which of the following amino acids is classified as a dicarboxylic amino acid?
All non-essential amino acids can be synthesized by the body.
All non-essential amino acids can be synthesized by the body.
Name two essential amino acids.
Name two essential amino acids.
__________ amino acids can be converted into glucose via gluconeogenesis.
__________ amino acids can be converted into glucose via gluconeogenesis.
Match the type of amino acid to their classification:
Match the type of amino acid to their classification:
Which amino acid carries a positive charge at physiological pH due to its protonated side chain?
Which amino acid carries a positive charge at physiological pH due to its protonated side chain?
Glutamic acid does not carry a negative charge at physiological pH.
Glutamic acid does not carry a negative charge at physiological pH.
What is the pK of Arginine, making it the most basic amino acid?
What is the pK of Arginine, making it the most basic amino acid?
Cysteine can form _______ bonds with another cysteine through oxidation.
Cysteine can form _______ bonds with another cysteine through oxidation.
Match the following amino acids with their corresponding formulas:
Match the following amino acids with their corresponding formulas:
Which of the following amino acids contains an imidazoline ring in its side chain?
Which of the following amino acids contains an imidazoline ring in its side chain?
Histidine is fully charged at physiological pH.
Histidine is fully charged at physiological pH.
What are the names given to aspartic acid and glutamic acid when they are ionized?
What are the names given to aspartic acid and glutamic acid when they are ionized?
The primary amino acid with a pK of ______ is Histidine.
The primary amino acid with a pK of ______ is Histidine.
Which amino acid is known for its ability to form cystine by bonding with another cysteine?
Which amino acid is known for its ability to form cystine by bonding with another cysteine?
Flashcards
What are proteins?
What are proteins?
Proteins are large biomolecules composed of one or more long chains of amino acid residues. They are essential for virtually all biological processes, including catalyzing metabolic reactions, DNA replication, transporting molecules across cell membranes, and providing structural support.
What is protein hydrolysis?
What is protein hydrolysis?
The breakdown of proteins into smaller units, specifically amino acids, using water and enzymes. This process is vital for digesting proteins and releasing amino acids that can be used by the body.
What are standard amino acids?
What are standard amino acids?
The 20 standard amino acids commonly found in proteins. They are encoded by DNA and differ in their chemical properties, contributing to the diverse functions and structures of proteins.
How are amino acids classified?
How are amino acids classified?
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Why do proteins contain nitrogen?
Why do proteins contain nitrogen?
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Are proteins polymers?
Are proteins polymers?
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What are the functions of proteins?
What are the functions of proteins?
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Non-polar Amino Acids
Non-polar Amino Acids
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Examples of Non-polar Amino Acids
Examples of Non-polar Amino Acids
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Glycine's Side Chain
Glycine's Side Chain
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Polar Amino Acids
Polar Amino Acids
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Examples of Polar Amino Acids
Examples of Polar Amino Acids
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Negatively Charged Amino Acids
Negatively Charged Amino Acids
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Positively Charged Amino Acids
Positively Charged Amino Acids
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Amino Acid Classification
Amino Acid Classification
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Glucogenic amino acids
Glucogenic amino acids
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Ketogenic amino acids
Ketogenic amino acids
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Glucogenic and ketogenic amino acids
Glucogenic and ketogenic amino acids
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Essential amino acids
Essential amino acids
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Non-essential amino acids
Non-essential amino acids
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Asparagine
Asparagine
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Glutamine
Glutamine
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Cysteine
Cysteine
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Cystine
Cystine
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Lysine
Lysine
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Arginine
Arginine
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Histidine
Histidine
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Glutamic acid
Glutamic acid
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Aspartic acid
Aspartic acid
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Charged Polar Amino Acids
Charged Polar Amino Acids
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What is Alanine?
What is Alanine?
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What is Valine?
What is Valine?
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What is Leucine?
What is Leucine?
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What is Isoleucine?
What is Isoleucine?
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What is Phenylalanine?
What is Phenylalanine?
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What is Methionine?
What is Methionine?
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What is Tryptophan?
What is Tryptophan?
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What is Proline?
What is Proline?
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What is Serine?
What is Serine?
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What is Threonine?
What is Threonine?
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Study Notes
Introduction to Amino Acids
- Amino acids are the building blocks of proteins.
- Proteins are large molecules with a high molecular weight, ranging from 5,000 to 25,000,000.
- Proteins can be broken down into smaller units called amino acids by hydrolysis.
- There are 20 standard amino acids.
- Proteins are unbranched polymers of L-α-amino acids.
- Amino acids are classified based on the polarity and charge of their R groups.
Protein Composition
- Proteins contain C, H, O, and N, with nitrogen comprising approximately 16% of their molecular weight.
- Other elements, such as I, Cu, Mn, Zn, and Fe, may also be present in small amounts.
- In 1839, Dutch chemist G.J. Mulder identified nitrogenous compounds in milk and eggs.
- Swedish scientist JJ Berzelius suggested the term "proteins" derived from the Greek word "proteios" meaning "primary" or "pre-eminent."
Amino Acids: Classification
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The 20 amino acids encoded by DNA are classified based on different criteria.
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One method is based on polarity and charge of their R groups.
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These groupings are:
- Non-polar
- Polar but uncharged
- Charged polar
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Another classification method is based on structures of side chains. This includes:
- Aliphatic amino acids
- Aromatic amino acids
- Heterocyclic amino acids
- Dicarboxylic amino acids
- Dibasic amino acids
- Imino acid
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A third way is based on catabolic fate, these are:
- Glucogenic
- Ketogenic
- Both glucogenic and ketogenic
Amino Acids: Classification-Cont
- Commonly, amino acids are classified based on their essential/non-essential nature.
- Essential Amino Acids: Cannot be synthesized by the body and must be obtained from the diet. These include valine, leucine, isoleucine, phenylalanine, threonine, tryptophan, methionine, and lysine.
- Nonessential Amino Acids: Can be synthesized by the body, and thus are not required in the diet. These include alanine, aspartic acid, asparagine, glycine, glutamic acid, glutamine, cysteine, proline, serine, and tyrosine.
- Semi-essential Amino Acid: These can be made by the body by they may not synthesize enough for optimal growth. Examples of semi-essential Amino Acids are arginine and histidine.
Non-standard Amino Acids
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These amino acids are formed from modifications of primary amino acids after protein synthesis.
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These modifications are vital for protein function.
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Examples include:
- Hydroxylysine and hydroxyproline (in collagen)
- Methylhistidine (muscle proteins)
- Phosphoserine (casein, enzymes)
- γ-carboxyglutamic acid (prothrombin, calcium-binding proteins)
- Pyroglutamic acid (N-terminal in thyrotropin, several proteins)
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Non-protein amino acids are found free in cells. Examples are ornithine and citrulline (urea cycle intermediates).
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Taurine is an abundant human amino acid found in bile (fat digestion and absorption)
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Other biologically important non-standard amino acids are used for functions beyond protein synthesis. Examples include chemical messengers (e.g., glycine, dopamine, GABA), local mediators of allergic reactions (e.g., histamine), and hormones (e.g., thyroxine).
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D-amino acids are components of bacterial cell walls and antibiotics.
New Amino Acids
- Selenocysteine is the 21st amino acid which is often part of several enzymes.
- Pyrrolysine is the 22nd amino acid and coded for by the UAG codon in some bacteria.
Functions of Amino Acids
- Amino acids serve various functions beyond serving as protein building blocks.
- Some amino acids are converted into carbohydrates (e.g., glucogenic amino acids).
- Other amino acids create specialized products; e.g.:
- Proteins which are hormones (e.g. thyroid hormones, epinephrine, norepinephrine and melanin)
- A vitamin, called niacin (B-vitamin) and serotonin from tryptophan
- Creatine from glycine, arginine, and methionine.
- Bile salts from glycine and cysteine.
- Others have a role in the synthesis of glutathione from glycine, cysteine, and glutamate.
- Histidine creates histamine on decarboxylation.
- Several amino acids, including aspartate and glutamine, are precursors for pyrimidine and purine biosynthesis.
- Methionine acts as an "active" methionine (SAM) transferring methyl groups to various molecules (transmethylation).
- Methionine and cysteine are sulfur sources.
Properties of Amino Acids
- Isomerism: Except glycine, all amino acids are optically active and exist in D and L forms. Naturally occurring proteins primarily contain L-forms.
- Amphoteric Nature and Isoelectric pH: Amino acids have an amino group (-NH2) and a carboxyl group (-COOH), making them capable of acting as both acids and bases. The isoelectric point (pI) is the pH at which an amino acid has no net charge.
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Description
Test your knowledge of proteins and amino acids with this engaging quiz. Explore various questions about the structure, classification, and properties of amino acids, and understand what makes proteins unique compared to carbohydrates and lipids. Perfect for students learning about biochemistry or molecular biology.