1: Amino Acids: Concept Summary Flashcards

1
Q

Amino Acids have four groups attached to a central (alpha) carbon: ______, _____, ______, ______

A

Amino group, Carboxylic Acid Group, Hydrogen Atom, R group

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2
Q

The _____ determines the chemistry and function of that amino acid.

A

R group

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3
Q

_______ amino acids appear in the proteins of eukaryotic organisms

A

Twenty

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4
Q

The stereochemistry of the alpha-carbon is _____ for all chiral amino acids in eukaryotes.

A

L

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5
Q

____-amino acids can exist in prokaryotes

A

D

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6
Q

All chiral amino acids except _____ have (S) configuration

A

cysteine

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7
Q

All amino acids are chiral except ____, which has a hydrogen atom as its R group

A

glycine

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8
Q

____ can be polar/nonpolar, aromatic/nonaromatic, charged/uncharged

A

Side chains

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9
Q

Nonpolar, nonaromatic amino acids: (7)

A

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline

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10
Q

Aromatic: (3)

A

Tryptophan, Phenylalanine, Tyrosine

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11
Q

Polar: (5)

A

Serine, Threonine, Asparagine, Glutamine, Cysteine

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12
Q

Negatively charged (acidic): (2)

A

Aspartate, Glutamate

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13
Q

Positively charged (basic): (3)

A

Lysine, Arginine, Histidine

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14
Q

Amino acids with __________ are hydrophobic

A

long alkyl chains

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15
Q

Amino acids with ______ are hydrophilic

A

charges

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16
Q

Amino acids are amphoteric. What does this mean?

A

they can accept or donate protons

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17
Q

The _____ of a group is the pH at which half of the species is deprotonated; [HA] = [A-]

A

pKa

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18
Q

T/F: Amino acids do not exist in different forms at different pH values.

A

False

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19
Q

At pH near the pI of the amino acid, the amino acid is ____________

A

a neutral zwitterion

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20
Q

At high (alkaline) pH, the amino acid is ___________

A

fully deprotonated

21
Q

The ____________ of an amino acid without a charged side chain can be calculated by averaging the two pKa values.

A

isoelectric point (pI)

22
Q

Amino acids can be _______.

A

titrated

23
Q

The titration curve is nearly _____ at the pKa values of the amino acid.

A

flat

24
Q

The titration curve is nearly _____ at the pI of the amino acid.

A

vertical

25
Q

Amino acids with charged side chains have an additional _______, and their pI is calculated by averaging the two pKa values that correspond to protonation and deprotonation of the zwitterion.

A

pKa value

26
Q

Amino acids without charged side chains have a pI of around ___.

A

6

27
Q

____ amino acids have a pI well below 6.

A

Acidic

28
Q

____ amino acids have a pI well above 6.

A

Basic

29
Q

_____ have two amino acid residues

A

Dipeptides

30
Q

_____ have three amino acid residues

A

Tripeptides

31
Q

_______ have a “few” amino acid residues (<20)

A

Oligopeptides

32
Q

______ have “many” amino acid residues (>20)

A

Polypeptides

33
Q

Forming a peptide bond is a ______ or _____ reaction (releasing 1 molecule of water).

A

condensation, dehydration

34
Q

The ______ amino group of one amino acid attacks the ______ carbonyl group of another amino acid.

A

nucleophilic amino

electrophilic carbonyl

35
Q

Amide bonds are rigid because of _____.

A

resonance

36
Q

Breaking a peptide bond is a ______ reaction.

A

hydrolysis

37
Q

______ is the linear sequence of amino acids in a peptide and is stabilized by peptide bonds.

A

Primary structure

38
Q

______ is the local structure of neighboring amino acids and is stabilized by hydrogen boding between amino groups and nonadjacent carboxyl groups

A

Secondary Structure

39
Q

____ are clockwise coils around a central axis

A

Alpha-helices

40
Q

__________ are rippled strands that can be parallel or antiparallel.

A

Beta-pleated sheets

41
Q

_____ can interrupt secondary structure because of its rigid cyclic structure

A

Proline

42
Q

________ is the 3D shape of a single polypeptide chain and is stabilized by hydrophobic interactions, acid-base interactions (salt bridges), hydrogen bonding, and disulfide bonds.

A

Tertiary Structure

43
Q

_______ push hydrophobic R groups to the interior or a protein, which increases entropy of the surrounding water molecules and creates a negative Gibbs free energy.

A

Hydrophobic Interactions

44
Q

_______ occur when two cysteine molecules are oxidized and create a covalent bond to form cystine.

A

Disulfide bonds

45
Q

________ is the interaction between peptides in proteins that contain multiple subunits.

A

Quaternary Structure

46
Q

Proteins with covalently attached molecules are termed _________

A

conjugated proteins

47
Q

The attached molecule in conjugated proteins are termed ______, and may be a metal ion, vitamin, lipid, carbohydrate or a nucleic acid

A

Prosthetic group

48
Q

Both heat and increasing solute concentration can lead to loss of 3D protein structure, which is termed _______

A

denaturation