WEEK 1 Flashcards
What are the 20 essential amino acids ? (list if they are non-polar, polar, + charged or - charged)
Non-polar:
Glycine
Alanine
Valine
Phenylalanine
Leucine
Isoleucine
Tryptophan
Cysteine
Proline
Methionine
Polar:
Serine
Threonine
Tyrosine
Asparagine
Glutamine
Acidic:
Aspartic Acid
Glutamic Acid
Basic:
Lysine
Histidine
Arginine
What is pI?
Isoelectric point. It is the point at which an amino acid is electrically neutral.
Describe the concept of acid-base chemistry (pH of solution to the pKa of the amino acid chain)
If the pH of the solution is less than the pKa of a functional group or side chain, then it will be PROTONATED.
If the pH of the solution is greater than the pKa of a functional group or side chain, then it will be DEPROTONATED
What is the pKa of the amino and carboxyl group of an amino acid ?
pKa amino group: ~9-10
pKa carboxyl group: ~2
What is a buffer ?
a solution that resists changes in pH when an acid or base is added
What are peptides?
a chain of multiple amino acids connected to each other via a dehydration reaction
What is a dehydration reaction? Describe its mechanism
a reaction that forms a bond while water is lost
mechanism: the carbon on the amino group nucleophilic attacks the carboxyl oxygen on the carboxyl group of the second amino acid forming a bond.
Is there any rotation about a peptide bond?
What are oligopeptides ?
What is hydrolysis ?
How do hydrolytic enzymes work ?
What does the primary structure of a protein tell us ?
How is the primary structure of a protein stabilized ?
What are covalent bonds ?
What does the secondary structure of an amino acid tell us?
How is the secondary structure of a protein stabilized ?
What are hydrogen bonds ?
What are the most common secondary structures of a protein and how are they stabilized ?
Describe the key structural differences between alpha helices and beta pleated sheets.
What is the function of proline in the secondary structure of a protein?
What does the tertiary structure of a protein tell us?
How is the tertiary structure of a protein stabilized ?
The 3D shape of a protein can be determined by ?
What is the important component found in the tertiary structure of a protein ?
What are disulfide bonds ? What reaction occurs during this process ?
What intermediate forms as the protein “collapses” into its tertiary structure ?
What process causes a protein to lose its function ?
Why do hydrophobic residues occupy the inferior part of a protein, while hydrophilic residues tend to accumulate on the exterior portion ?
What is a solvation layer ?
What would ΔS be if a hydrophobic side chain is placed in an aqueous solution ?
