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Biochemistry Flashcards

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MCAT flashcards
1
Q

Amino acids

A

Molecules that contain an a amino group, a carboxyl group, a hydrogen atom, and a side chain/R group

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2
Q

Side chain/R group

A

Specific to each amino acid

Determines the properties and functions of amino acids

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3
Q

Proteinogenic amino acids

A

The 20 a-amino acids encoded by the human genetic code

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4
Q

What are the proteinogenic amino acids?

A

Alanine, Arginine, Asparagine, Aspartic acid, Cysteine, Glutamic acid, Glutamine, Glycine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Proline, Serine, Threonine, Tryptophan, Tyrosine, and Valine

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5
Q

Glycine, Gly, G

A

Smallest amino acid
Only achirl amino acid
Nonpolar, nonaromatic side chain
Has H as its R group

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6
Q

Alanine, Ala, A

A

Nonpolar, nonaromatic side chain

1 carbon alkyl side chain

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7
Q

Valine, Val, V

A

Nonpolar, nonaromatic side chain

3 carbon alkyl side chain

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8
Q

Leucine, Leu, L

A

Nonpolar, nonaromatic side chain

4 carbon alkyl side chain

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9
Q

Isoleucine, Ile, I

A

Nonpolar, nonaromatic side chain

4 carbon alkyl side chain

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10
Q

Methionine, Met, M

A

Nonpolar, nonaromatic side chain
1 of 2 amino acids with a sulfur in its side chain
Sulfur has a methyl group attached

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11
Q

Proline, Pro, P

A

Nonpolar, nonaromatic side chain

Amino nitrogen becomes part of the side chain and creates a 5 membered ring

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12
Q

Tryptophan, Trp, W

A

Uncharged aromatic side chain

Double-ring system that contains a nitrogen

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13
Q

Phenylalanine, Phe, F

A

Uncharged aromatic side chain
Benzyl side chain (benzene + CH2)
Relatively nonpolar

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14
Q

Tyrosine, Tyr, Y

A

Uncharged aromatic side chain
Phenylalanine with an added Oh group on the benzene ring
Relatively polar

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15
Q

Serine, Ser, S

A

Polar, nonaromatic side chain
CH2 + OH side chain
Able to participate in hydrogen bonding

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16
Q

Threonine, Thr, T

A

Polar, nonaromatic side chain
CH3 + C + OH side chain
Able to participate in hydrogen bonding

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17
Q

Asparagine, Asn, N

A

Polar, nonaromatic side chain

CH2 + amide side chain

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18
Q

Glutamine, Gln, Q

A

Polar, nonaromatic side chain

CH2 + CH2 + amide side chain

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19
Q

Cysteine, Cys, C

A

Polar, nonaromatic side chain
CH2 + thiol side chain
Sulfur in side chain is prone to oxidation

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20
Q

Aspartic acid, Asp, D

A

Negatively charged (acidic) side chain
CH2 + carboxylate side chain
Anion is aspartate

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21
Q

Glutamic acid, Glu, E

A

Negatively charged (acidic) side chain
CH2 + CH2 + carboxylate side chain
Anion is glutamate

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22
Q

Lysine, Lys, K

A 
Positively charged (basic) side chain
Terminal primary amino group
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23
Q

Arginine, Arg, R

A 
Positively charged (basic) side chain
3 nitrogens in its side chain
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24
Q

Histidine, His, H

A 
Positively charged (basic) side chain
Aromatic ring with 2 nitrogen atoms in its side chain (imidazole)
25
Q

Amphoteric species

A

A species that can either accept or donate a proton depending on the pH of their environment

26
Q

Isoelectric point (pI)

A

The pH at which the molecule is electrically neutral (zwitterion)

27
Q

pI for neutral amino acids

A

Calculated by averaging the pKa values for the amino and carboxyl groups
(pKa,NH3 group + pKa,COOH group)/ 2

28
Q

pI for acidic amino acids

A

Calculated by averaging the pKa values for the R and carboxyl groups
(pKa,R group + pKa,COOH group)/ 2

29
Q

pI for basic amino acids

A

Calculated by averaging the pKa values for the amino and R groups
(pKa,NH3+ group + pKa,R group)/ 2

30
Q

Peptides

A

Composed of amino acid residues

31
Q

Dipeptides

A

Consist of 2 amino acid residues

32
Q

Tripeptides

A

Consist of 3 amino acid residues

33
Q

Oligopeptides

A

Relatively small peptides

Up to about 20 amino acid residues

34
Q

Polypeptides

A

Longer chain of amino acid residues

35
Q

Peptide bonds

A

The bond that joins the residues in peptides
Specialized form of an amide bond that forms between the COO- group of one amino acid and the NH3+ group of another amino acid
Example of condensation/dehydration reaction

36
Q

Condensation/dehydration reaction

A

Results in the removal of a water molecule

37
Q

Proteins

A

Polypeptides that range from just a few amino acids in length up to thousands

38
Q

Primary protein structure

A

Linear arrangement of amino acids coded in an organism’s DNA

Stabilized by the covalent bonds between adjacent amino acids

39
Q

Sequencing

A

Laboratory technique used to determine the primary structure of a protein

40
Q

Secondary protein structure

A

The local structure of neighboring amino acids

Result of hydrogen bonds between nearby amino acids a-helices and B-pleated sheets

41
Q

a-helices

A

Rodlike structure in which the peptide chain coils clockwise around a central axis
Stabilized by intramolecular hydrogen bonds

42
Q

Keratin

A

Fibrous structural protein found in human hair, skin, and fingernails
a-helix is an important component in the structure

43
Q

B-pleated sheets

A

Peptide chains lie alongside one another forming rows or strands
Stabilized by intramolecular hydrogen bonds

44
Q

Fibrous proteins

A

Structure resembles sheets or long strands

Collagen

45
Q

Globular proteins

A

Structure is spherical

Myoglobin

46
Q

Tertiary protein structure

A

3D shape
Determined by hydrophilic and hydrophobic interactions between R groups of amino acids
Van der Waals forces, hydrogen bonds, ionic bonds, and covalent bonds

47
Q

Disulfide bonds

A

Present in tertiary protein structure
Form when two cysteine molecules between oxidized to form cystine
Create loops in the protein chain

48
Q

Molten globules

A

Intermediate state in between the secondary structure and the tertiary structure

49
Q

Denaturation

A

When the 3D structure of protein is changed, causing the protein to no longer function

50
Q

Solvation layer

A

Formed by nearby solvent molecules when a solute dissolved in a solvent

51
Q

Quaternary protein structure

A

Only exist for proteins that contain more than one polypeptide chain
An aggregate of smaller globular peptides and represents the functional form of the protein
Van der Waals forces, hydrogen bonds, ionic bonds, and covalent bonds

52
Q

Cooperativity/allosteric effects

A

One subunit can undergo conformational or structural changes, which can either enhance or reduce the activity of the other subunits

53
Q

Conjugated proteins

A

Proteins with covalently attached molecules called prosthetic groups

54
Q

Prosthetic groups

A

Small molecules permanently attached to the enzyme
Can be organic molecules (vitamins) or metal ions (iron)
Direct proteins to be delivered to certain locations

55
Q

Lipoproteins

A

Proteins with lipid prosthetic groups

56
Q

Glycoproteins

A

Proteins with carbohydrate prosthetic groups

57
Q

Nucleoproteins

A

Proteins with nucleic acid prosthetic groups

58
Q

Heme

A

Iron-based, pigment part of hemoglobin

MCAT Prep (8 decks)

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