Amino Acids Flashcards

(49 cards)

1
Q

Building blocks of protein

A

Amino acids

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2
Q

Composed of alpha carbon

A

Amino acids

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3
Q

Unique to each amino acids

A

R (side chain)

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4
Q

Can act both as an acid and base

A

Amphoteric

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5
Q

Accepts hydrogen atom

A

Amino group

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6
Q

Donate hydrogen atom

A

Carboxyl group

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7
Q

Both positively and negatively charged amino acids

A

Zwitterion

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8
Q

Almost all amino acids

A

L-amino acids

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9
Q

Can be seen in cell walls / antiobiotics

A

D-amino acids

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10
Q

Connects amino acids to produce protein

A

Peptide bond

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11
Q

Used in protein synthesis

A

Magic 20 amino acids

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12
Q

Dependent on R chain

A

Chemical nature

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13
Q

Amino acids that synthesized by the body

A

Non-essential amino acids

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13
Q

Must be acquired thru diet

A

Essential amino acids

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14
Q

Synthesized in adequate amounts by adults, but supplemented in newborns

A

Semi-essential amino acids

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15
Q

Used to generate glucose thru gluconeogenesis

A

Glucogenic amino acids

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16
Q

Used to generate ketone bodies

A

Ketogenic amino acids

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17
Q

Used as an alternative energy source

A

Ketone bodies

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18
Q

Hydrophobic amino acids

A

Nonpolar and uncharged

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19
Q

Hydrophilic amino acids

A

Polar & uncharged

20
Q

Are fundamental units of proteins

21
Q

Simple molecules containing both a amine group and an acid group

22
Q

Magic 20 is labeled by

A

Francis crick & James Watson

23
Q

He determined the structure of DNA

A

Francis Crick & James Watson

24
This makes amino acids water-soluble
Zwitterion
25
It is protaned, giving the amino acid a positive charge
Carboxylate group
26
It is the pH at which an amino acid exists in its zwitterion form (equal amounts of protonated and deprotonated forms)
Isoelectric point
27
It is deprotonated, the amino acid giving a negative charge
Ammonium group
28
Molecules with a chiral carbon atom are optically active, meaning they can rotate plane polarized light
Chiral molecules
29
Only chiral amino acid, due to having two hydrogen atoms attached to the a-carbon
Glycine
30
Only forms found in proteins
L-amino acids
31
Found in some antibiotic and bacterial cell walls
D-amino acids
32
A way to represent the arrangement of groups around a chiral carbon atom
Fischer projection
33
These amino acids can hydrogen bond with water, making them more soluble than nonpolar amino acids
Polar and uncharged amino acids
34
A weaker acid than the primary carboxylic acid group in the Amino acid backbone
Secondary carboxylic acid group
35
It is important for interactions with metal ions, acting as nucleophiles in enzymes, and in ionic interactions
Side chain
36
It forms the guanidinium group
Arginine
37
It has a simple ammonium ion as its basic group
Lysine
38
Forms an imidazolium group
Histidine
39
These are found in collagen and gelatin
Hydroxylysine and hydroxyproline
40
Nonpolar side chains clump together due to London dispersion forces. They exclude water and other side chains.
Hydrophobic interactions
41
Polar and uncharged side chains interact through hydrogen bonding with water and each other.
Hydrophilic interactions
42
Acidic and basic side chains with opposite charges attract. A carboxylate group from one side chain can form an ionic bond with the ammonium ion of another side chain.
Ionic interactions
43
Two cysteine molecules can form a disulfide linkage through a mild oxidation reaction.
Disulfide linkages
44
A protein is a chain of at least now many amino aids joined together
150
45
Is a crucial bond in biochemistry, formed between two amino acids through A dehydration reaction
Peptide bond
46
Product of two amino acids joined by peptide bond
Dipeptide
47
a flat, planar structure stabilized by resonance.
Peptide bond
48
formed by adding a third amino acid to a dipeptide.
Tripeptide