Amino acids, Peptides, Proteins, and Enzymes

Question 1

Amino acids contain which two functional groups?

Answer 1

Amino group

Carboxyl group

Question 2

Amino acid stereochemistry is ____________ (exceptions?)

Answer 2

Chiral (4 different groups attached to it)

Glycine - has a H attached as its R group (achiral)

Question 3

All chiral amino acids are configured __________ (exceptions?)

Answer 3

L-amino acids

Cysteine has an L-structure with R configuring

Question 4

Nonpolar, nonaromatic amino acids

Answer 4

Glycine
Alanine
Valine
Leucine
Isoleucine
Methionine
Proline

Question 5

Aromatic side chain amino acids

Answer 5

Tryptophan
Phenylalanine
Tyrosine

Question 6

Polar amino acids

Answer 6

Serine
Threonine
Asparagine
Glutamine
Cysteine

Question 7

Acidic side chain amino acids

Answer 7

Aspartic acid

Glutamic acid

Question 8

Basic amino acids

Answer 8

Lysine
Arginine
Histidine

Question 9

Amino acids are ___________

Answer 9

Amphoteric

Zwitterions

Question 10

Isoelectric point (pI)

Answer 10

The pH where the molecule is electrically neutral.

pI = sum pKa of both amine and carboxyl group over 2

Question 11

Amino acid subunits

Answer 11

Peptides

Also termed residues

Question 12

Dipeptide

Answer 12

Two amino acid residues

Question 13

Tripeptides

Answer 13

3 amino acids joined

Question 14

Peptide bond formation

Answer 14

Condensation or dehydration

Question 15

Condensation

Answer 15

Peptide bond formation

Question 16

Hydrolysis

Answer 16

Peptide bond cleavage

Question 17

Primary

Answer 17

His-Leu-Iso-Pro

Letters

Question 18

Secondary

Answer 18

Alpha helices
Beta sheets

Words

Question 19

Tertiary

Answer 19

Folded proteins

Sentences

Question 20

Quaternary

Answer 20

Complex dense proteins

Paragraphs

Question 21

These types of proteins derive part of their function from covalently attached molecules…

Answer 21

Conjugated proteins

Question 22

Prosthetic groups

Answer 22

Can be organic molecules

Examples: vitamins or metals

Question 23

Opposite of protein folding

Answer 23

Denaturation

Question 24

Key features of Enzymes

Answer 24

Lower activation energy
Increase rate of reaction
Do not alter equilibrium constant
Are not consumed in reaction
Are pH and temp sensitive
Do not effect Gibbs free energy
Are reaction specific

Question 25

Enzyme classification

Answer 25

LIL HOT Ligase Isomerase Lyase Hydrolase Oxido-reductase Transferase

Question 26

Oxidoreductase

Answer 26

Catalyze oxidation-reduction reactions

Question 27

Transferase

Answer 27

Transfer functional groups

Question 28

Hydrolase

Answer 28

Break a compound into two molecules

Question 29

Lyase

Answer 29

Break one molecule into two

Question 30

Isomerase

Answer 30

rearrange bonds within molecules

Question 31

Ligases

Answer 31

Catalyze addition or synthesis reactions

Question 32

Energy input reaction

Answer 32

Endergonic

Question 33

Energy given off

Answer 33

Exergonic

Question 34

Enzymes without their cofactors

Answer 34

Apoenzymes

Question 35

Enzymes containing their cofactors

Answer 35

Holoenzymes

Question 36

HIGH Km = ??

Answer 36

LOWER affinity because it requires a higher substrate concentration **the opposite is also true

Question 37

Cooperative enzymes Allosteric enzymes

Answer 37

Sigmoidal kinetics

Question 38

Optimal temp for enzymes

Answer 38

37 degrees Celsius

Question 39

Optimal pH

Answer 39

7.4

Question 40

Competitive Inhibition

Answer 40

Same 1/v | Different 1/[S]

Question 41

Noncompetitive Inhibition

Answer 41

Same 1/[S] | Different 1/v

Question 42

Inactive enzymes

Answer 42

Zymogens