Amino Acids Overview and Classification

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Questions and Answers

Which property is NOT characteristic of amino acids?

They are insoluble in water. (correct)

They have high melting points.

They decompose upon heating.

They are colorless, crystalline solids.

What type of amino acids must be obtained through diet?

Essential amino acids (correct)

Non-essential amino acids

Biosynthetic amino acids

Conditional amino acids

Which of the following is a common symptom of amino acid deficiency?

Enhanced digestion

Skin and hair problems (correct)

Heightened cognitive function

Increased energy levels

What is the maximum number of amino acids in a peptide?

Less than 50 amino acids Signup and view all the answers

Which function is NOT typically performed by proteins?

Storing genetic information Signup and view all the answers

What type of bond connects amino acids together in a protein?

Peptide bond Signup and view all the answers

Which group contains amino acids with specific structural roles?

Structural components Signup and view all the answers

What are olig peptides comprised of?

2 to 20 amino acids Signup and view all the answers

What type of bond links amino acids in proteins?

Peptide bond Signup and view all the answers

Which process breaks down proteins and peptides into smaller peptides or amino acids?

Proteolysis Signup and view all the answers

What is the role of chaperone proteins?

To assist in protein folding Signup and view all the answers

Which of the following describes the linear sequence of amino acids?

Primary structure Signup and view all the answers

What occurs during denaturation of proteins?

Loss of function and structure Signup and view all the answers

What is the significance of protein-protein interactions (PPI)?

They establish functional collaborations between proteins Signup and view all the answers

Which structural feature is stabilized by hydrogen bonds in proteins?

Local folding patterns Signup and view all the answers

What is the primary outcome of renaturation in proteins?

Reconstruction of native structure Signup and view all the answers

What are the key elements that make up amino acids?

Carbon, Hydrogen, Oxygen, Nitrogen Signup and view all the answers

Which group of amino acids cannot be synthesized by the body and must be obtained from food?

Essential Signup and view all the answers

What is a zwitterion?

A molecule with functional groups that have distinct charges Signup and view all the answers

At which pH does an amino acid have an overall charge of zero?

Isoelectric Point Signup and view all the answers

Under strongly acidic conditions, how does an amino acid behave?

It gains a proton and acts as a base. Signup and view all the answers

How are amino acids classified as conditionally essential?

They are usually synthesized by the body but needed during specific circumstances. Signup and view all the answers

Which part of the general structure of an amino acid is unique to each amino acid?

R group (side chain) Signup and view all the answers

In strong alkaline conditions, what happens to an amino acid?

It loses a proton and behaves as an acid. Signup and view all the answers

What characterizes the primary difference between non-covalent and covalent interactions?

Covalent interactions involve the sharing of electrons, while non-covalent interactions do not. Signup and view all the answers

Which protein is NOT mentioned as being used in medical applications?

Collagen Signup and view all the answers

What role do enzymes play in biochemical reactions?

Enzymes act as biocatalysts that speed up reactions without being consumed. Signup and view all the answers

How do enzymes achieve specificity in substrate binding?

Through the active site shape matching the substrate’s shape. Signup and view all the answers

Which of the following describes the structure of enzymes?

Enzymes can be composed of multiple polypeptide chains in a complex. Signup and view all the answers

What is the primary function of keratin in personal care products?

To strengthen hair and improve its structure. Signup and view all the answers

The lock-and-key model and the induced fit model are related to which of the following?

The way substrates bind to an enzyme's active site. Signup and view all the answers

Which proteins are mentioned as beneficial for plant growth in agriculture?

Protein-rich plant food for soil microbes Signup and view all the answers

What describes the lock-and-key model of enzyme interaction?

Substrates fit into enzymes like a key fits into a lock. Signup and view all the answers

Which statement accurately describes enzyme catalysis?

Enzymes stabilize the substrates and accelerate the reaction rate. Signup and view all the answers

What is a key application of enzymes in the food industry?

They assist in the tenderization of meat. Signup and view all the answers

How do non-competitive inhibitors function?

They bind to an allosteric site, altering enzyme activity. Signup and view all the answers

Which of the following accurately defines competitive inhibition?

The inhibitor resembles the substrate and competes for the active site. Signup and view all the answers

What role do enzymes play in waste management?

They contribute to the degradation of pollutants. Signup and view all the answers

What does the induced fit model propose about enzyme activity?

The active site can adjust its conformation to better fit the substrate. Signup and view all the answers

How are protease inhibitors utilized in medicine?

They can prevent the replication of viruses like HIV. Signup and view all the answers

Study Notes

Amino Acids

Amino acids are organic compounds that combine to form proteins.
They are the building blocks of proteins.
Key elements are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N).
There are approximately 300 amino acids found in nature.
The general formula of an amino acid is R-CH(NH2)-COOH.
An amino acid has a basic amino group (-NH2), an acidic carboxyl group (-COOH), and a unique R group (or side chain).
"Amino acid" is short for α-amino carboxylic acid (α-amino).

Structure of Amino Acids

Specific structures and chemical formulas are provided for various amino acids (e.g., Glycine, Alanine, Serine, etc). Refer to the provided images for details.

Classification of Amino Acids

Amino acids are categorized into three groups:
- Essential: Cannot be produced by the body, must be obtained from food.
- Non-essential: Can be produced by the body.
- Conditionally essential: Typically not essential, except during illness or stress.
Specific examples of amino acids in each category are listed. Refer to the provided image for details.

Acid-Base Properties

Each amino acid has an isoelectric point (pI) where the overall charge on the amino acid molecule is zero.
Examples of isoelectric points are provided for various amino acids (e.g., aspartic acid, glycine, histidine, arginine).
A zwitterion is a molecule with at least one positive and one negative charge.
In acidic conditions, the carboxyl group gains a proton and the amino acid acts as a base.
In alkaline conditions, the amino group loses a proton and the amino acid acts like an acid.

Physical Properties

Amino acids are colorless, crystalline solids.
They have a high melting point.
Soluble in water, slightly soluble in alcohol, and with difficulty in methanol, ethanol, and propanol.
They decompose upon heating to high temperatures.
All amino acids (except glycine) are optically active.
A peptide bond links amino acids.

Sources of Amino Acids

Amino acids perform various biological and chemical functions in the body, including building/repairing tissues, enzyme function, digestion etc.
The body synthesizes some amino acids.
Other amino acids (essential amino acids) need to be consumed through protein-rich foods.

Deficiency of Amino Acids

Amino acid deficiencies can cause various health problems, including edema, anemia, insomnia, diarrhea, depression, hypoglycemia, loss of appetite, fat deposits in the liver, and skin/hair problems.

Proteins

Proteins are large biomolecules composed of one or more chains of amino acid residues.
One of the most abundant organic molecules in living organisms.
Perform diverse functions (e.g., structural components, catalysts [enzymes], hormones, and regulators of cellular processes).
Proteins are involved in DNA replication, molecule transportation, and catalyzing various metabolic reactions, as well as structural support to cells.
Proteins are broken down into amino acids.

Peptides and Proteins

Peptides: Chains of fewer than 50 amino acids.
- Oligpeptides: 2 to 20 amino acids.
- Dipeptides and Tripeptides: 2 and 3 amino acids.
Proteins: Chains of more than 50 amino acids. Typically 100-10,000 amino acids linked together.
Amino acids are joined by peptide bonds.
Edman Degradation is a method to sequence amino acids in peptides.

Amino Acids that Make Up Proteins

Lists amino acid names and structures.

General Structure of Proteins

The general formula for proteins is RCH(NH2)COOH.
Proteins have primary, secondary, tertiary, and quaternary structures.
Primary structure: The linear sequence of amino acids.
Secondary structure: Folding patterns (e.g., α-helix, β-pleated sheet) stabilized by hydrogen bonds.
Tertiary structure: The 3D shape of the protein.
Quaternary structure: The arrangement of multiple polypeptide chains into a functional enzyme complex (e.g., hemoglobin).

Protein Folding and Misfolding

Protein folding is the process by which a linear chain of amino acids folds into a 3D structure.
Chaperones assist in protein folding.
Denaturation is the loss of a protein's 3D structure, usually caused by heat, pH changes, or chemicals.
Renaturation is possible if the denaturation process isn´t too severe.
Misfolding can lead to diseases like Alzheimer's, Parkinson's, Huntington's and Creutzfeldt-Jakob.

Protein-Protein Interactions

Protein-Protein Interactions (PPI) are the physical contact between two or more protein molecules.
Interactions can be non-covalent and covalent.

Protein Applications

Many proteins, like insulin and antibodies, are used in medicine.
Proteins (e.g., casein, whey, soy protein) are used in food products (e.g., dairy alternatives, protein bars).
Proteins (e.g., keratin) are utilized in personal care products.

Enzymes

Enzymes are biological catalysts that speed up biochemical reactions without being consumed.
All biochemical reactions in cells require enzymes.
Enzymes are typically proteins.
Some RNA molecules (ribozymes and DNAzymes) can also act as catalysts.

Structure of Enzymes

Enzymes have primary, secondary, tertiary, and quaternary structures.
The primary structure defines the enzyme's function.
Secondary structures (like α-helices and β-sheets) provide stability.
Tertiary structures provide the 3D shape necessary for substrate binding and catalysis.
Quaternary structure involves multiple polypeptide chains.

Active Site

The active site is the region of an enzyme where the substrate binds and catalytic activity occurs.
Enzyme specificity relates to the active site fitting with the specific substrate.
The amino acid residues in the active site determine the precise function of the enzyme.

Enzyme Mechanism of Action

Lock-and-key model describes enzymes and substrates as having complementary shapes, while the induced fit model proposes enzymes adjust their shape to fit substrates precisely.
Enzyme-substrate complex is when enzyme and substrate interact.
Both models explain how enzymes interact with their substrates to facilitate chemical reactions.

Enzyme Catalysis

Enzymes increase the rate of chemical reactions by lowering the activation energy.
Enzymes stabilize the transition state of the reaction (to make it proceed easily).

Industrial and Biotechnological Applications

Enzymes are used in various industries:
Biocatalysis: Enzyme use in pharmaceuticals, fine chemicals, and biofuels.
ELISA: Enzyme-based diagnostic methods.
Food industry: Proteases and amylases in various food processes.
Waste management: Enzyme use in waste remediation.

Enzyme Inhibitors and Drugs

Enzyme inhibitors are molecules that bind to enzymes and decrease their activity.
Competitive, non-competitive, and uncompetitive are types of reversible inhibitors.
Inhibitors can be used as therapeutic agents to treat diseases.
Allosteric inhibitors can turn off enzymes by binding to different sites to change the enzyme´s shape.

Three Types of Reversible Inhibition

Competitive inhibitors: Bind to the enzyme's active site, preventing substrate binding.
Non-competitive inhibitors: Bind to a site other than the active site, changing the enzyme's shape.
Uncompetitive inhibitors: Bind only to the enzyme-substrate complex, preventing the reaction.
Allosteric inhibitors: Bind to a specific site, altering the enzyme's shape.

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Description

This quiz covers the fundamentals of amino acids, including their structure, functions, and classification. Learn about essential, non-essential, and conditionally essential amino acids, as well as their roles as building blocks of proteins. Test your knowledge on this crucial topic in biochemistry.