Unit Two - Biochemistry - Protein

Question 1

What are the five elements that make up proteins?

Answer 1

Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur

Question 2

What are the monomers of proteins?

Answer 2

Amino Acids

Question 3

What is the structure of Amino Acids?

Answer 3

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

Question 4

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

Answer 4

1. The Base of the Amino Acid
2. Nitrogen bonded to 2 Hydrogen
   (-NH2)

Question 5

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

Answer 5

1. 20 Different R - Groups
2. The variable group
3. Provides unique properties that distinguishes amino acids from each other
4. Chemical Nature (polar, nonpolar, acidic, basic)
5. CN determines the AA’s relationships in a protein

Question 6

4 different types of R - Groups?

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)

Answer 7

1. In plants
2. Addition of an amine group
3. To an organic molecule
4. Creating an amino acid

Question 8

What are essential amino acids? (2)

Answer 8

1. Amino Acids that the body cannot create on its own
2. Must be from your diet in order to obtain the EAA

Question 9

Definition of Transamination (2)

Answer 9

1. Creation of NONessential amino acids
2. An amine group is transferred from one AA to a keto acid

Question 10

Definition of Deamination (4)

Answer 10

1. We cannot store excess amino acids in our body
2. Convert them through remvoing the amine group
3. Occurs in the Liver
4. Converted into Ammonia, and the rest is pooped out

Question 11

Definition of Denature

Answer 11

To permenantly change the 3D shape of a protein

Question 12

What are factors that contribute to denature?

Answer 12

1. Change the Heat
2. Change the pH level
   (The changes affect the hydrogen bonding)

Question 13

Definition of Peptide Bonds

Answer 13

Bond formed between amino acids after DS

Question 14

What are the functions of protein? (6)

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 amino acids bonded togehtrer

Question 16

Defintinition of a Polypepetide

Answer 16

3 or more amino acids bonded together (Protein)

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?

Answer 19

1. Some AA are also linked by H - Bonds due to the attraction of some partially + and partially - atoms
2. Folds into an alpha - helix shape or pleated sheet

Question 20

What is the tertiary structure of proteins?

Answer 20

1. More attractions are present
2. Making the 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 amino acids 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.