Amino Acids Flashcards
Students should know the structures, properties, names and shorthand (three and one letter codes) for the 20 amino acids.
In humans, __(L or D) amino acids are the building blocks of proteins, and there are __ (#) official amino acids coded in the human genome.
L
20 (22 if we include the random ones from the lecture)
AA: Nonpolar, Hydrophobic, Small
Glycine, Alanine
Why is glycine important?
In collagen triple helixes, every 3rd AA is Gly. Creates tighteness.
AA: Nonpolar, Hydrophobic, Larger
Valine, Leucine, Isoleucine, Methionine
Name the branched chain amino acids and explain their significance.
Valine, Leucine, Isoleucine.
Maple Syrup Urine Disease is caused by the bodies inability to breakdown these AAs.
Why is Methionine significant?
- Methionine is the start codon AUG in RNA translation to proteins.
- Met acts as a Methyl Group Donor because of its Sulfur.
AA: Nonpolar, Hydrophobic, Weird
Proline; Proline plays a central role in the FORMATION of alpha helices and beta sheets. While proline’s unique structure may also disrupt both alpha helixes and beta sheets, it’s ability to make sharp turns facilitates the FORMATION of both structures, with proline commonly being found at the beginning of alpha helices or at the turns in beta sheets.
AA: Nonpolar, Hydrophobic, Aromatic
Phenylalanine, Tryptophan
AA: Nonpolar, Hydrophilic, Aromatic
AA: Polar, Hydrophilic
Serine, Threonine
Polar, Disulfide Bond
Cysteine
- Cysteine’s side chain is capable of forming a disulfide bridge (becoming cystine), which is a covalent bonds between 2 sulfur atoms through side chain oxidation and removal of 2 hydrogen atoms.
- Cysteine is in the free form when in a reducing environment (intracellular space; full of antioxidants, cytoplasm)
- Cysteine is in the disulfide bond when in an oxidizing environment (extracellular space)
*When in the reducing cytoplasm, cysteins are happy and alone. When in an oxidizing environment, the cysteine get scared and hold hands. *
AA: Negatively Charged and their Polar derivatives
Aspartate, Glutamate; Asparagine, Glutamine
AA: Positively Charged
Histidine (pI of 6 )
Lysine (pI of 11)
Arginine (pKA of 12)
Why is lysine significant in the context of DNA and epigenetics?
Histones bind to negatively charged DNA through their positively charged Lysine residues. Methylating or Acetylating the Lysines opens DNA to increase gene expression.
Which amino acids can be phosphorylated?
Which ones have -OH groups?
- Tyrosine
- Serine
- Threonine