MY AMINO ACIDS

• 20 amino acids

  - serine (Ser, S)

  - threonine (Thr, T)

  - tyrosine (Tyr, Y)

  - asparagine (Asn, N)

  - glutamine (Gln, Q)

  - lysine (Lys, K)

  - arginine (Arg, R)

  - histidine (His, H)

  - aspartic acid (Asp, D)

  - glutamic acid (Glu, E)

  - alanine (Ala, A)

  - valine (Val, V)

  - proline (Pro, P)

  - phenylalanine (Phe, F)

  - glycine (Gly, G)

  - cysteine (Cys, C)

  - leucine (Leu, L)

  - isoleucine (Ile, I)

  - methionine (Met, M)

  - tryptophan (Trp, W)
• polar amino acids

  serine, threonine, tyrosine, asparagine, glutamine
• basic (charged) amino acids

  lysine, arginine, histidine
• acidic (charged) amino acids

  aspartic acid, glutamic acid
• hydrophobic nonpolar amino acids

  alanine, valine, proline, phenylalanine, glycine, cysteine, leucine, isoleucine, methionine, tryptophan
• serine


  - Ser, S

  - polar (alcohol)

  
• threonine


  - Thr, T

  - polar (alcohol)

  
• tyrosine


  - Tyr, Y

  - polar (alcohol)

  - aromatic

  
• asparagine


  - Asn, N

  - polar (amide)

  
• glutamine


  - Gln, Q

  - polar (amide)

  
• lysine


  - Lys, K

  - basic

  
• arginine


  - Arg, R

  - basic

  
• histidine


  - His, H

  - basic

  
• aspartic acid


  - Asp, D

  - acidic

  
• glutamic acid


  - Glu, E

  - acidic

  
• alanine


  - Ala, A

  - nonpolar

  - methyl group

  
• valine


  - Val, V

  - nonpolar

  - isopropyl group

  
• proline


  - Pro, P

  - nonpolar

  - attaches to N on backbone

  
• phenylalanine


  - Phe, F

  - nonpolar

  - aromatic

  
• glycine


  - Gly, G

  - nonpolar

  - simplest - just H

  
• cysteine


  - Cys, C

  - nonpolar

  - forms disulfide bonds

  
• leucine


  - Leu, L

  - nonpolar

  
• isoleucine


  - Ile, I

  - nonpolar

  
• methionine


  - Met, M

  - nonpolar

  - has S, but no disulfide bonds

  
• tryptophan


  - Trp, W

  - nonpolar

  - aromatic

  
• valine, leucine and isoleucine are all similar in their methyl groups
• phenylalanine and tryptophan both have carbon rings in thier side chains
• asparatic acid and glutamic acid both have a methyl group and then a carboxyl group with an oxygen
• lysine and arginine are similar in having three methyl groups with an amide group
• serine and threonine both have methyl and hydroxyl groups
• asparagine and glutamine both have methyl, carboxyl, and amide groups
• 🍋 alanine

  • hydrophobic, similar to serine
  • found in transmembrane helices that anchor proteins into the membrane
• 🍉 valine

  Val - V

  • part of the EEVD-COO- motif that allows HOP to recognize both HSP70 and HSP90
• 🍊 leucine

  Leu - L

  • if it is the second amino acid, then an E3 ligase will recognize it and target the protein for degradation (n-end rule)
  • has an extra carbonyl group
  • found in transmembrane helices that anchor proteins into the membrane
• 🥝 isoleucine

  Ile - I

  • if it is the second amino acid, then an E3 ligase will recognize it and target the protein for degradation (n-end rule)
• 🍍 proline

  Pro - P

  • peptidyl-prolyl isomerase is a chaperone that is specific to prolines
  • can engage in cis and trans formations
• 🥭 phenylalanine

  Phe - F

  • if it is the second amino acid, then an E3 ligase will recognize it and target the protein for degradation (n-end rule)
  • change from phenylalanine to serine is pathogenic (very different)
  • found in transmembrane helices that anchor proteins into the membrane
• 🍑 methionine

  Met - M

  • is the starting amino acid for protein synthesis
• 🍓 tryptophan

  Trp - W

  • if it is the second amino acid, then an E3 ligase will recognize it and target the protein for degradation
• 🍒Cysteine (Cys) can form disulfide bonding, which occurs in the exterior of the cell (ER lumen) but not in the reducing environment (cytosol), creating covalent bonds that stabilize the protein's structure