Unit Two - Biochemistry - Protein

Question 1

What are the five elements that make up proteins?

Answer 1

C, H, N, O, S

Question 2

What are the monomers of proteins?

Answer 2

Amino Acids

Question 3

What is the structure of Amino Acids? (3)

Answer 3

1. Amino Group
2. R - Group
3. Carboxyl Group

Question 4

What is the amino group in Amino Acids? (2)

Function, Structure

Answer 4

1. Base of AA
2. N bonded to 2 H
   (-NH2)

Question 5

What is the R - Group in Amino Acids? (5)

Answer 5

1. Variable Group
2. Provides Distinguishable Properties
3. Chemical Nature (NP, P, Acidic, Basic)
4. Cn Determines AA relationships in the protein
5. 20 Different R - Groups

Question 6

4 different types of R - Groups?

Read Through

Answer 6

Hydroxyl Group

R-group: OH

Polar

Alanine (Ala, A):

R-group: CH₃ (a methyl group)

Nonpolar

Serine (Ser, S):

R-group: CH₂OH (a hydroxyl group)

Polar and participates in hydrogen bonding.

Cysteine (Cys, C).

R-group: CH₂SH (a thiol group)

Function: The sulfur atom allows cysteine to form disulfide bonds, which are crucial for stabilizing protein structures.

Aspartic Acid (Asp, D): The R-group (CH₂COOH) is acidic and can donate a proton, making it negatively charged at physiological pH, enabling it to form ionic bonds.

Question 7

Definition of Amination (4)

Occurs in, Process, Product

Answer 7

1. Found in plants
2. Addition of amine group
3. To organic molecule
4. Forms AA

Question 8

What are essential amino acids? (2)

Answer 8

1. AA the body cannot create
2. Obtained through diet

Question 9

Definition of Transamination (4)

Location, Product, Process

Answer 9

1. In Body
2. Forms Nonessential AA
3. Amine group from AA
4. Transferred to keto acid

Question 10

Definition of Deamination (4)

Cause, Process, Products & Occurs in

Answer 10

1. Excess AA cannot be stored
2. Amine Group is Removed
3. Converted to Ammonia & Waste
4. Occurs in the Liver

Question 11

Definition of Denature

Answer 11

1. Permenantly change the 3D shape of a protein
2. Affects H - Bonding

Question 12

What are factors that contribute to denature? (2)

Answer 12

1. Change in heat
2. Change in pH
   (The changes affect the hydrogen bonding)

Question 13

Definition of Peptide Bonds (2)

Definition & Formation

Answer 13

1. Bond between AA
2. Formed from Dehydration Synthesis

Question 14

What are the functions of protein? (6)

Read Through

Answer 14

1. Structural Support: Keratin strengthens tissue
2. Speeds up Chemical Reactions: Amylase breaks down starches
3. Transport: Hemoglobin transports O2 in the blood
4. Defense: Immunoglobin
5. Regulation: Insulin regulates blood sugar levels.
6. Movement: Actin and Myosin are involved in muscle contraction

Question 15

Definition of Dipeptide

Answer 15

Two bonded AA

Question 16

Defintinition of a Polypepetide

Answer 16

3 or more bonded AA

Ex: Protein

Question 17

What are the four structures of a protein?

Answer 17

1. Primary
2. Secondary
3. Tertiary
4. Quatenary

Question 18

What is the primary structure of proteins?

Answer 18

Sequence of AA connected by peptide bonds

Question 19

What is the secondary structure of proteins? (2)

Answer 19

1. Some AA linked by H - Bonds due to Dipoles
2. Folded into an alpha - helix/pleated sheet

Question 20

What is the tertiary structure of proteins? (2)

Answer 20

1. More attractions are present
2. Makes shape 3D

Question 21

What are the bonds that creates the tertiary structure of protein? (3)

Answer 21

1. Disulfide Bonds: Covalent Bonds between Sulfur Atoms in R - Groups (Ex: SH)
2. Hydrophobic Interactions: Hydrophobic particles cluster together on the inside of the protein (Ex: CH3)
3. Ionic Bonds: Fully charged AA form ionic bonds pulling toward each other (OH)

Question 22

What is the quaternary structure of proteins?

Answer 22

Multiple proteins come together to form a larger and more complex structure.