SBI4U1

Protein Equations

1. Complete the reactions below, name each amino acid, and answer accompanying
questions.

Type of reaction: _________________________

2.
+

Type of reaction: _______________________

3.
+

Type of reaction: _______________________

4.
+

Type of reaction: _______________________

5. For each peptide below, use an arrow to point out the peptide bond(s) and name each
amino acid.
1. What groups of atoms are found in all amino acids?
Proteins and Nucleic Acids
Answer: Amino group (-NH₂), carboxyl group (-COOH), hydrogen atom, and a variable R
group . • Proteins are polymers composed of amino acids folded into specific 3D structures.
• Functions of proteins include structural support, transport, signaling, immune defense, and
catalyzing reactions (enzymes).
2. Describe the difference between the primary and secondary protein structures.
Answer: • Nucleic acids (DNA and RNA) are responsible for storing and transmitting genetic
information.
• Primary structure: The unique sequence of amino acids in a polypeptide chain. • DNA passes hereditary information, while RNA plays a key role in protein synthesis.

• Secondary structure: Repeated folding or coiling of the polypeptide chain into alpha-helices or Amino Acids
beta-pleated sheets, stabilized by hydrogen bonds . • All amino acids contain a central carbon atom bonded to:
• An amino group (-NH₂)

3. Explain why it is necessary for a protein to adopt specific tertiary and quaternary • A carboxyl group (-COOH)
arrangements. • A hydrogen atom
Answer: Tertiary and quaternary structures are critical because they determine the protein’s • A variable R group (which determines the amino acid’s properties)
three-dimensional shape, which is essential for proper function . • There are 20 amino acids, classified as:
• Non-polar: Hydrophobic side chains
4. Explain the role of hydrogen bonding and disulfide bonds between R groups.
• Polar: Hydrophilic side chains
Answer:
• Charged: Acidic (-COOH) or basic (-NH₂)
• Hydrogen bonds: Stabilize the secondary and tertiary structures by forming between partially
positive and negative atoms. Protein Structure

• Disulfide bonds: Covalent bonds formed between the sulfur atoms of two cysteine side groups, Proteins have up to four levels of structure:
providing additional structural stability . 1. Primary Structure:
• Linear sequence of amino acids
• Alteration in even one amino acid can affect function.
5. List some of the different types of proteins and their functions. Identify specific applications
of these proteins in various living organisms. 2. Secondary Structure:

Answer: • Coils (alpha-helix) or folds (beta-pleated sheet) stabilized by hydrogen bonds.

3. Tertiary Structure:
• Structural proteins: Provide support (e.g., keratin in hair).
• Overall 3D shape determined by interactions between R groups.

• Defensive proteins: Protect against infections (e.g., antibodies). • Includes hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.
4. Quaternary Structure:
• Signal proteins: Function as messengers (e.g., insulin hormone).
• Assembly of multiple polypeptide chains (e.g., hemoglobin with four subunits).
• Carrier proteins: Transport molecules (e.g., hemoglobin carries oxygen).
Peptide Bonds
• Enzymes: Speed up chemical reactions (e.g., amylase breaks down starch) . • Peptide bonds link amino acids through dehydration synthesis, forming polypeptide
chains.
• A polypeptide is a chain longer than 50 amino acids.
7. A researcher finds a protein solution has a pH above 7.
• Proteins only function properly after folding into their final 3D shape.

(a) What amino acids would you predict to be abundant in this protein? Why? Protein Types and Functions
Answer: Basic amino acids, such as lysine, arginine, and histidine, are abundant since they raise
1. Structural Proteins: Provide physical support (e.g., keratin, collagen).
the pH by accepting protons .
2. Defensive Proteins: Fight infections (e.g., antibodies).

(b) What amino acids would you predict to be uncommon in this protein? Why? 3. Signal Proteins: Regulate processes (e.g., hormones like insulin).
Answer: Acidic amino acids, such as aspartic acid and glutamic acid, are uncommon since they 4. Carrier Proteins: Transport molecules (e.g., hemoglobin).
lower the pH by donating protons . 5. Enzymes: Catalyze biochemical reactions (e.g., amylase).
6. Motile Proteins: Enable movement (e.g., actin and myosin).
9. Explain the similarities and differences between DNA and RNA.
Answer: Nucleic Acids
• Two types: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).
• Similarities: Both are polymers of nucleotides composed of a sugar, phosphate group, and
nitrogenous base. • Nucleotides are the building blocks, consisting of:
• A nitrogenous base (A, T, G, C for DNA; A, U, G, C for RNA)
• Differences: DNA contains deoxyribose and thymine, while RNA contains ribose and uracil . • A five-carbon sugar (deoxyribose in DNA, ribose in RNA)
• One to three phosphate groups
10. Draw the linkage of two nucleotides and two amino acids. • DNA forms a double helix structure with complementary base pairing:
Answer: • A pairs with T (or U in RNA), and G pairs with C.
• RNA is single-stranded and can fold into various structures.
• Nucleotide linkage: A phosphodiester bond between the 3’ carbon of one sugar and the 5’
phosphate group of the next nucleotide.
Nitrogenous Bases

• Amino acid linkage: A peptide bond formed between the carboxyl group of one amino acid • Purines: Adenine (A) and Guanine (G) (double-ring structure)
and the amino group of another, releasing a water molecule . • Pyrimidines: Cytosine (C), Thymine (T), and Uracil (U) (single-ring structure)

Phosphodiester Bonds
13. Select one essential amino acid. Describe its function, sources, and symptoms of deficiency. • Link nucleotides to form the sugar-phosphate backbone of nucleic acids.
Answer:
• DNA strands are antiparallel (opposite directions).
• Example: Lysine
Key Vocabulary
• Function: Essential for collagen formation and calcium absorption. • Amino acid: Monomer unit of proteins.
• Protein: Polymer of amino acids with structural and functional roles.
• Sources: Meat, dairy, eggs, and legumes.
• Nucleotide: Building block of nucleic acids.
• Deficiency symptoms: Poor growth, fatigue, and immune dysfunction . • Peptide bond: Covalent bond linking amino acids.
• Denaturation: Loss of protein structure and function due to external stress (e.g., pH,
temperature).

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