Amino Acids Flashcards
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
essential vs. non-essential amino acids
Essential- must be obtained by diet:
* Valine
* Leucine
* Isoleucine
* Phenylalanine
* Tryptophan
* Threonine
* Lysine
* Methionine
* Histidine
*memorise
Vampires Love Incredibly Pointy Teeth Like Mighty Hungry Tigers
Non-essential- body can produce:
* Alanine
* Arginine
* Asparagine
* Aspartic acid
* Cysteine
* Glutamic acid
* Glutamine
* Glycine
* Proline
* Serine
* Tyrosine
primary/secondary/tertiary/quaternary structures of proteins
Primary: sequence of AA
- peptide bonds
Secondary: alpha helix/beta sheets
Tertiary: forms “blob”
Quaternary: multi AA (oligomers-subunits)
where are proteins?
Enzymes - signaling and growth
Structure - collagen, actin, tubulin (muscles and movement)
Cell signaling
Channel proteins - in and out of nucleus or cell (membranes)
how many amino acids are there? how many are essential?
20
9 essential
the aromatic ring on Tyrosine gives ______ qualities
hydrophobic
the hydroxyl group on Tyrosine give ____
polarity
(can be partially or fully charged - negative)
general structure of AA
Amino, Carboxylic acid, hydrogen atom, R-group
what AA doesn’t have chirality?
Glycine
four different R-groups
Hydrophobic
Hydrophilic
Charged
Special
Hydrophobic AAs (water hating)
inside of proteins
Glycine
Alanine
Valine
Leucine
Isoleucine
Tryptophan
Phenylalanine
Get - glycine
Away - alanine
Vile - valine
Liquid - leucine
I - isoleucine
Trusted - tryptophan
Phyou - phenylalanine
Hydrophilic AAs (water loving)
near surface of protein
Threonine
Asparagine
Serine
Glutamine
Three - threonine
Asparagus - asparagine
See - serine
water - -philic
God - glutamine
Charged AA
at the surface
Aspartic acid
Tyrosine
Arginine
Lysine
Glutamic acid
Aspire - aspartic acid
To - tyrosine
Argue - arginine
Like - lysine
Glut - glutamic acid
Special AAs
Proline - usually at sharp turns
Cysteine - disulfide bonds in keratin (form/breaks)
Methionine - no sulfide bonds but important for active sites
Histidine - buffering, N+ or uncharged
ketogenic vs glucogenic vs both AAs
Ketogenic:
- Lysine
- Leucine
Glucogenic:
- Alanine
- Arginine
- Asparagine
- Cysteine
- Glutamine
- Glycine
- Histidine
- Methionine
- Proline
- Serine
- Valine
Both:
- Isoleucine
- Phenylalanine
- Threonine
- Tyrosine
- Tryptophan
