Amino Acids Flashcards

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

A

Amino acids

21
Q

Simple molecules containing both a amine group and an acid group

A

Amino acids

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
Q

This makes amino acids water-soluble

A

Zwitterion

25
Q

It is protaned, giving the amino acid a positive charge

A

Carboxylate group

26
Q

It is the pH at which an amino acid exists in its zwitterion form (equal amounts of protonated and deprotonated forms)

A

Isoelectric point

27
Q

It is deprotonated, the amino acid giving a negative charge

A

Ammonium group

28
Q

Molecules with a chiral carbon atom are optically active, meaning they can rotate plane polarized light

A

Chiral molecules

29
Q

Only chiral amino acid, due to having two hydrogen atoms attached to the a-carbon

A

Glycine

30
Q

Only forms found in proteins

A

L-amino acids

31
Q

Found in some antibiotic and bacterial cell walls

A

D-amino acids

32
Q

A way to represent the arrangement of groups around a chiral carbon atom

A

Fischer projection

33
Q

These amino acids can hydrogen bond with water, making them more soluble than nonpolar amino acids

A

Polar and uncharged amino acids

34
Q

A weaker acid than the primary carboxylic acid group in the Amino acid backbone

A

Secondary carboxylic acid group

35
Q

It is important for interactions with metal ions, acting as nucleophiles in enzymes, and in ionic interactions

A

Side chain

36
Q

It forms the guanidinium group

A

Arginine

37
Q

It has a simple ammonium ion as its basic group

A

Lysine

38
Q

Forms an imidazolium group

A

Histidine

39
Q

These are found in collagen and gelatin

A

Hydroxylysine and hydroxyproline

40
Q

Nonpolar side chains clump
together due to London dispersion
forces. They exclude water and
other side chains.

A

Hydrophobic interactions

41
Q

Polar and uncharged side chains interact
through hydrogen bonding with
water and each other.

A

Hydrophilic interactions

42
Q

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.

A

Ionic interactions

43
Q

Two cysteine molecules can form a disulfide
linkage through a mild oxidation
reaction.

A

Disulfide linkages

44
Q

A protein is a chain of at least now many amino aids joined together

A

150

45
Q

Is a crucial bond in biochemistry, formed between two amino acids through A dehydration reaction

A

Peptide bond

46
Q

Product of two amino acids joined by peptide bond

A

Dipeptide

47
Q

a flat, planar structure stabilized by resonance.

A

Peptide bond

48
Q

formed by adding a third amino acid to a dipeptide.

A

Tripeptide