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Human Form & Function > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

What bond connects AAs into a primary structure?

A

Peptide bonds

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2
Q

What amino acid helps with sharp angles?

A

Proline - usually at sharp turns

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3
Q

Glucogenic AAs

A

Aspartate
Asparagine
Alanine
Arginine
Cysteine
Glycine
Glutamate
Gutamine
Histidine
Methionine
Serine
Valine

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4
Q

Glucogenic and ketogenic amino acids

A

T, P, I (except proline) = both Glu and Keto

Tryptophan
Tyrosine
Phenylalanine
Threonine
Isoleucine

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5
Q

Ketogenic Amino Acids

A

Lysine
Leucine

Starts with L= ketogenic

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6
Q

Where are proteins?

A

Enzymes: Signaling and growth
Structure: Collagen, actin/tubulin

cell signaling

Channel proteins: in and out of cells or nucleus

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7
Q

How does collagen hold its structure?

A

Glycine - small so allows for compaction

Hydroxy proline and hydroxy lysine help with stability and form.

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8
Q

Collagen structure

A

Triple helix protein

Glycine every 3 AAs
smaller AA
Hydroxy-proline and -lysine (stability/form)

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9
Q

Protein structures

A

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)

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10
Q

Ketogenic amino acids

A

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 :(

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11
Q

Glucogenic amino acids

A

Glucogeninc amino acids turned into glucose via gluconeogenesis

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12
Q

Special AAs

A

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.

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13
Q

Charged AAs

A

Positive or negatively charged at the surface of protein

Tyrosine (-) O¯
Aspartic acid (-) COO¯
Glutamic acid (-) COO¯
Lysine (+) NH3+
Arginine (+) NH2+

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14
Q

Hydrophilic AAs

A

On or near the surface of a protein often near activation site

Serine (-)
Threonine (-)
Asparagine(+)
Glutamine(+)

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15
Q

Hydrophobic AAs

A

Water avoiding

Inside of proteins

Glycine
Alanine
Valine
Leucine
Isoleucine
Phenylalanine
Trypotphan

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16
Q

4 R-Groups

A

Hydrophobic

Hydrophilic

Charged

Special

17
Q

Does glycine have chirality?

A

No

Glycine is the only AA that doesn’t have chirality

Glycine is the smallest AA

18
Q

Stereoisomers

A

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

19
Q

General structure of amino acids

A

Central carbon with these attached:
1. Amino group
2. Carboxylic acid
3. Hydrogen atom
4. R-group (Makes them different)

20
Q

Essential amino acids

A

Must be obtained by diet

Valine
Leucine
Isoleucine
Phenylalanine
Tryptophan
Threonine
Lysine
Methionine
Histidine

21
Q

Conditionally essential amino acids

A

During times of growth, pregnancy, disease (change)

The body cannot produce the required amount so needs more

22
Q

Non-essential amino acids

A

The human body can produce on its own

23
Q

Tyrosine side note…

A

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)

24
Q

Why do Amino acids matter in dentistry?

A

Proteins are building blocks for many things in dentistry:
- Periodontal health
- Enzymatic reactions
- cell signaling

Also nutrition and growth

25
Q

essential vs. non-essential amino acids

A

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

26
Q

primary/secondary/tertiary/quaternary structures of proteins

A

Primary: sequence of AA
- peptide bonds
Secondary: alpha helix/beta sheets
Tertiary: forms “blob”
Quaternary: multi AA (oligomers-subunits)

27
Q

where are proteins?

A

Enzymes - signaling and growth

Structure - collagen, actin, tubulin (muscles and movement)

Cell signaling

Channel proteins - in and out of nucleus or cell (membranes)

28
Q

how many amino acids are there? how many are essential?

A

20
9 essential

29
Q

the aromatic ring on Tyrosine gives ______ qualities

A

hydrophobic

30
Q

the hydroxyl group on Tyrosine give ____

A

polarity

(can be partially or fully charged - negative)

31
Q

general structure of AA

A

Amino, Carboxylic acid, hydrogen atom, R-group

32
Q

what AA doesn’t have chirality?

A

Glycine

33
Q

four different R-groups

A

Hydrophobic
Hydrophilic
Charged
Special

34
Q

Hydrophobic AAs (water hating)

A

inside of proteins

Glycine
Alanine
Valine
Leucine
Isoleucine
Phenylalanine
Tryptophan

35
Q

Hydrophilic AAs (water loving)

A

near surface of protein

Serine
Threonine
Asparagine
Glutamine

36
Q

Charged AA

A

at the surface

Tyrosine
Aspartic acid
Glutamic acid
Lysine
Arginine

37
Q

Special AAs

A

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

38
Q

ketogenic vs glucogenic vs both AAs

A

Ketogenic:
- Lysine
- Leucine

Glucogenic:
- Alanine
- Arginine
- Asparagine
- Cysteine
- Glutamine
- Glycine
- Histidine
- Methionine
- Proline
- Serine
- Valine

Both:
- Isoleucine
- Phenylalanine
- Threonine
- Tyrosine
- Tryptophan

39
Q
A

Human Form & Function (21 decks)

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