Amino Acids Flashcards
(39 cards)
What bond connects AAs into a primary structure?
Peptide bonds
What amino acid helps with sharp angles?
Proline - usually at sharp turns
Glucogenic AAs
Aspartate
Asparagine
Alanine
Arginine
Cysteine
Glycine
Glutamate
Gutamine
Histidine
Methionine
Serine
Valine
Glucogenic and ketogenic amino acids
T, P, I (except proline) = both Glu and Keto
Tryptophan
Tyrosine
Phenylalanine
Threonine
Isoleucine
Ketogenic Amino Acids
Lysine
Leucine
Starts with L= ketogenic
Where are proteins?
Enzymes: Signaling and growth
Structure: Collagen, actin/tubulin
cell signaling
Channel proteins: in and out of cells or nucleus
How does collagen hold its structure?
Glycine - small so allows for compaction
Hydroxy proline and hydroxy lysine help with stability and form.
Collagen structure
Triple helix protein
Glycine every 3 AAs
smaller AA
Hydroxy-proline and -lysine (stability/form)
Protein structures
Primary: sequence of AA, peptide bonds (makes H2O, condensation)
Secondary: alpha-helix and beta-sheet
Tertiary: Forms “blob”, folding and interactions between alpha-helix and beta-sheets
Quaternary: multiple subunits (oligomers)
Ketogenic amino acids
Ketogenic amino acids turned into ketone bodies
Ketone bodies: float in blood (water soluble) fatty acids and AA
Via ketosis: no carbohydrates so uses keto AA for energy
or
Ketoacidosis: diabetic, high levels of ketone bodies which makes body acidic :(
Glucogenic amino acids
Glucogeninc amino acids turned into glucose via gluconeogenesis
Special AAs
Proline: Sharp turns, easy to contort and fit
Cysteine: disulfide bonds, form and break reversible, keratin (perms➡︎stinky➡︎S)
Methionine: no sulfide bonds. important for active sites
Histidine: uncharged or positive N’s important for buffering.
Charged AAs
Positive or negatively charged at the surface of protein
Tyrosine (-) O¯
Aspartic acid (-) COO¯
Glutamic acid (-) COO¯
Lysine (+) NH3+
Arginine (+) NH2+
Hydrophilic AAs
On or near the surface of a protein often near activation site
Serine (-)
Threonine (-)
Asparagine(+)
Glutamine(+)
Hydrophobic AAs
Water avoiding
Inside of proteins
Glycine
Alanine
Valine
Leucine
Isoleucine
Phenylalanine
Trypotphan
4 R-Groups
Hydrophobic
Hydrophilic
Charged
Special
Does glycine have chirality?
No
Glycine is the only AA that doesn’t have chirality
Glycine is the smallest AA
Stereoisomers
Mirror images
Both L-isomers and D-isomers have been found in humans
L-isomers - COMMON
D-isomers in mutations, cancer, disease post modification from enzymatic reactions
General structure of amino acids
Central carbon with these attached:
1. Amino group
2. Carboxylic acid
3. Hydrogen atom
4. R-group (Makes them different)
Essential amino acids
Must be obtained by diet
Valine
Leucine
Isoleucine
Phenylalanine
Tryptophan
Lysine
Methionine
Histidine
Threonine
Vampires - valine
Love - leucine
Intensley - Isoleucine
Pointy - phenylalanine
Teeth - tryptophan
Like - lysine
Mighty - methylalanine
Hungry - Histidine
Tigers - threonine
Conditionally essential amino acids
During times of growth, pregnancy, disease (change)
The body cannot produce the required amount so needs more
Non-essential amino acids
The human body can produce on its own
Tyrosine side note…
Tyrosine has an aromatic ring that gives hydrophobic qualities (nonpolar, hates water)
It can be charged partially or fully negative because of the hydroxyl group (gives polarity)
Why do Amino acids matter in dentistry?
Proteins are building blocks for many things in dentistry:
- Periodontal health
- Enzymatic reactions
- cell signaling
Also nutrition and growth
