Lecture 3: Amino Acid Structures Flashcards
1
Q
Amino Acids and Protein Structure
A
- 20 amino acids that have distinct side chains that contribute to protein structure and function
- Non-covalent and covalent interactions between functional groups are important for holding protein together + interactions
- Interaction of hydrophilic amino acids with water help solubilize some proteins
2
Q
Amino acids
A
- Amino acids made up of an amino group, carboxyl group, and R side chain
3
Q
Chiral amino acids
A
- Asymetric alpha carbon results in chirality
- Chiral molecules are non-superimposable mirror images
- L amino acids are found in plant and animal proteins
4
Q
Non-covalent interactions
A
- Hydrogen bonds can form between hydroxyl, carboxyl, thiol, and amino groups
- Hydrogen bonds can form between amino acid side chains with protein structure
- Can occur between aliphatic and hydrophobic side chains
5
Q
Disulfide bonds
A
- Disulfide bonds covalently cross-link two cysteines together
- Disulfide bridges can be interchain or between different polypeptide chains
- Linkages stabilize structures
- Protein Disulfide Isomerase enzymes help catalyze oxidation reaction
- Disulfide bonds can be broken by reducing agents in cytosol or in lab(B-mercaptoethanol)
6
Q
Hydrophobic Amino Acids
A
- Hydrophobic amino acids can be found in the interior of proteins, maximizing number of hydrophilic interactions with water
- Hydrophobic amino acids can still be found on surface to allow for non-covalent interactions
7
Q
Post Translational Modification
A
- Additional or removal of functional groups can change structure of a protein and affect its function
- Disulfide bond formation is example of PTM