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Flashcards

Biochem Amino Acids

paige redmond English 24 cards

Aspartate (asp, D) negatively charged at pH=7 aspartic acid when not ionized has 2 carboxylic groups

Cards in this deck (24)

  1. 1Charged R-groupamino acids ionizable side chain
    (asp, glu, lys, arg, his)
  2. 2Hydrophilic R-groupamino acids with side chain polar, not ionized
    (ser,thr,cys,gln)
  3. 3Hydrophobic R-groupamino acid without side chain polar groups
    (gly, ala, pro, val, leu, ile, met)
  4. 4Aromatic R-groupamino acid with large cyclic ring side chains
    (phe, tyr, trp)
  5. 5—Aspartate
    (asp, D)
    negatively charged at pH=7
    aspartic acid when not ionized
    has 2 carboxylic groups
    Aspartate (asp, D) negatively charged at pH=7 aspartic acid when not ionized has 2 carboxylic groups
  6. 6—Glutamate
    (glu,E)
    negatively charged at pH=7
    neurotransmitter
    glutamic acid when hydrogen bond to R-group
    Glutamate (glu,E) negatively charged at pH=7 neurotransmitter glutamic acid when hydrogen bond to R-group
  7. 7—Lysine
    (lys,K)
    positively charged at pH=7
    side chain of 4 aliphatice carbins, with terminal amino group
    Lysine (lys,K) positively charged at pH=7 side chain of 4 aliphatice carbins, with terminal amino group
  8. 8—Arginine
    (arg, R)
    positively charged at pH=7
    side chain 3 aliphatic carbons with terminal guanidino group
    double bonded NH2+ bonded to central carbon is guanidino group
    Arginine (arg, R) positively charged at pH=7 side chain 3 aliphatic carbons with terminal guanidino group double bonded NH2+ bonded to ce...
  9. 9—Histidine
    (his, H)
    positively charged or neutral at pH=7
    imidazole group can gain or lose hydrogen ion to become + or neutral
    enzymes use histadine at active sited b/c it can become deprotonated or protonated
    Histidine (his, H) positively charged or neutral at pH=7 imidazole group can gain or lose hydrogen ion to become + or neutral enzymes use...
  10. 10—Cysteine
    (cys, C)
    sulfhydryl group can for disulfide bonds
    disulfide bonds within protein or btw protein is important for stabilizing protein structure
    Cysteine (cys, C) sulfhydryl group can for disulfide bonds disulfide bonds within protein or btw protein is important for stabilizing pro...
  11. 11—Threonine
    (thr, T)
    hydroxyl group can hydrogen bond and be phosphorylated
    contains both methyl and hydroxyl group
    Threonine (thr, T) hydroxyl group can hydrogen bond and be phosphorylated contains both methyl and hydroxyl group
  12. 12—Serine
    (ser,S)
    hydrogen bond donor, phosphorylated
    enzymes within cell can add or remove phosphate groups to control protein function
    Serine (ser,S) hydrogen bond donor, phosphorylated enzymes within cell can add or remove phosphate groups to control protein function
  13. 13—Asparagine
    (asn, N)
    high degree of hydrophilic
    amine group and carbonyl group that can hydrogen bond
    Asparagine (asn, N) high degree of hydrophilic amine group and carbonyl group that can hydrogen bond
  14. 14—Glutamine
    (gln,Q)
    amino group and carbonyl group that can hydrogen bond
    important for nitrogen transport through body
    Glutamine (gln,Q) amino group and carbonyl group that can hydrogen bond important for nitrogen transport through body
  15. 15—Isoleucine
    (lle,I)
    Methyl group attached to one branch
    Isoleucine (lle,I) Methyl group attached to one branch
  16. 16—Leucine
    (leu, L)
    most abundant amino acid
    4 carbons as side chain
    Leucine (leu, L) most abundant amino acid 4 carbons as side chain
  17. 17—Glycine
    (gly, G)
    smallest by mass
    no chiral alpha carbon- achiral
    Glycine (gly, G) smallest by mass no chiral alpha carbon- achiral
  18. 18—Methionine
    (met, M)
    sulfur atom cannot hydrogen bond and cannot for disulfide bridges
    first amino acid for all proteins during synthesis
    Methionine (met, M) sulfur atom cannot hydrogen bond and cannot for disulfide bridges first amino acid for all proteins during synthesis
  19. 19—Phenylalanine
    (phe, F)
    plays role in neurotransmitting and pigment synthesis
    hydrophobic
    Phenylalanine (phe, F) plays role in neurotransmitting and pigment synthesis hydrophobic
  20. 20—Alanine
    (ala, A)
    side chain methyl group
    most common amino acid found in proteins
    Alanine (ala, A) side chain methyl group most common amino acid found in proteins
  21. 21—Proline
    (pro, P)
    form pyrrolidine ring
    ring causes kink/bend at proline residues
    side chain carbon swings around tho bond with amino nitrogen
    Proline (pro, P) form pyrrolidine ring ring causes kink/bend at proline residues side chain carbon swings around tho bond with amino nitr...
  22. 22—Valine
    (val, V)
    V-shapped carbons
    important in protein synthesis in muscle cells, consumed by athletes as nutritional supplement
    Valine (val, V) V-shapped carbons important in protein synthesis in muscle cells, consumed by athletes as nutritional supplement
  23. 23—Tyrosine
    (tyr,Y)
    hydroxyl group allows hydrogen bonds
    found at transition from hydrophobic to hydrophilic
    Tyrosine (tyr,Y) hydroxyl group allows hydrogen bonds found at transition from hydrophobic to hydrophilic
  24. 24—Tryptophan
    (trp, W)
    has indole side chain
    largest amino acid by mass
    indole group nitrogen can hydrogen bond
    Tryptophan (trp, W) has indole side chain largest amino acid by mass indole group nitrogen can hydrogen bond

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Flashcards on Biochem Amino Acids, created by paige redmond on 09/09/2020.
Created by
paige redmond
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