Biochemistry: Proteins, Purines, And Pyrimidines

Front 1

What are 4 non-cavalent functional group interactions found in proteins?

Back 1

hydrogen bonds
electrostatic/ionic interactions
hydrophobic interactions
van der Waal interactions

Front 2

Where does a peptide bond form?

Back 2

between the carboxyl and amino groups

Front 3

In which direction is a protein read?

Back 3

N-terminus to C-terminus

Front 4

What are 2 covalent functional group interactions found in proteins?

Back 4

peptide bonds
disulfide bonds

Front 5

What mutation causes sickle cell anemia?

Back 5

change in the Beta-subunit at position #6 from glutamate to valinne, eliminating the negative charge

Front 6

How is an alpha-hlix stabilized?

Back 6

hydrogen bonds from an amino group to the carboxyl group that is located 4 amino acids away

Front 7

How is a Beta-sheet stabilized?

Back 7

hydrogen bonds from an amino group to the carboxyl group on the neighboring strand

Front 8

Which amino acids are found in Beta-bends?

Back 8

proline and glycine

Front 9

What are 3 examples of fibrous tertiary structire?

Back 9

alpha-keratin
collagen
silk

Front 10

What kind of structure does alpha-keratin have?

Back 10

left-handed triple helix made up of right-handed helices

Front 11

What kind of structure does collagen have?

Back 11

right-handed triple helix made up of left-handed helices

Front 12

What is the repeating sequence in collagen?

Back 12

glycine - proline- Y (hydroxyproline/hydroxylysine)

Front 13

What kind of structure does silk have?

Back 13

Beta-sheet

Front 14

What is the repeating sequence in silk?

Back 14

glycine - alanine - glycine - alanine - glycine - serine

Front 15

What is an important characteristic of globular proteins?

Back 15

water-soluble

Front 16

How is collagen stabilized?

Back 16

hydrogen bonds between helices
covalent bonds between lysine and hydroxylysine

Front 17

How is keratin stabilized?

Back 17

hydrogen bonds within a helix
hydrophobic interactions and disulfide bonds between helices

Front 18

What is often required for protein renaturation?

Back 18

chaperones

Front 19

What does cooperative binding mean for hemoglobin?

Back 19

binding of each oxygen increases the oxygen affinity of the remaining subunits

Front 20

What shifts the Hb-O2 curve to the right?

Back 20

2-3 BPG
hydrogen
high temperature

Front 21

What shifts the Hb-O2 curve to the left?

Back 21

fetal hemoglobin (HbF)
CO

Front 22

What is the result of sickle cell anemia?

Back 22

hemolysis

Front 23

What are 3 reversible covalent modifications?

Back 23

phosphorylation
methylation
acetylation

Front 24

What makes up a nucleoside?

Back 24

sugar + base

Front 25

What makes up a nucleotide?

Back 25

sugar + base + phosphate group

Front 26

Which position in a pyrimidine binds carbon 1 of the sugar?

Back 26

N1

Front 27

Which position in a purine binds carbon 1 of the sugar?

Back 27

N9

Front 28

What is the preferred conformation of a nucleoside's Beta-glycosidic bond?

Back 28

anti

Front 29

What does endo refer to for a sugar pucker?

Back 29

that carbon lies above the plane

Front 30

What does exo refer to for a sugar pucker?

Back 30

that carbon lies below the plane

Front 31

Where are unusual amino acids found?

Back 31

sythesized (AZT)
tRNA

Front 32

What is AZT used as a treatment for?

Back 32

HIV

Front 33

How does AZT work?

Back 33

terminated DNA replication by blocking thymidine

Front 34

What does purine biosynthesis start with?

Back 34

phosphoribosyl pyrophosphate (PRPP)

Front 35

What is needed to build a purine ring?

Back 35

amino acids

Front 36

What donates a methyl group in purine biosynthesis?

Back 36

tetrahydropholic acid (THF)

Front 37

What is the first purine formed in the biosynthesis pathway?

Back 37

IMP

Front 38

What is needed to make GTP?

Back 38

ATP

Front 39

What is needed to make ATP?

Back 39

GTP

Front 40

What inhibits the first step in purine biosynthesis?

Back 40

AMP, ADP, ATP
GMP, GDP, GTP

Front 41

What substance regulates ATP synthesis?

Back 41

ATP

Front 42

What substance regulates GTP synthesis?

Back 42

GTP

Front 43

Deficiency of what enzyme leads to severe combined immunodeficiency syndrome (SCIDS)?

Back 43

adenosine deaminase

Front 44

What does adenosine deaminase do?

Back 44

degrades AMP

Front 45

What does a deficiency of adenosine deaminase cause?

Back 45

SCIDS

Front 46

What causes Gaut?

Back 46

high levels of urate

Front 47

What does high levels of urate cause?

Back 47

Gaut

Front 48

A deficiency of what enzyme causes Lesch Nyhan Syndrome?

Back 48

HGPRT

Front 49

What does a deficiency in HGPRT cause?

Back 49

Lesch Nyhan Syndrome (excess urate)

Front 50

What are the characteristics of Lesch Nyhan Syndrome?

Back 50

self-mutilation
gaut
aggressiveness
mental retardation

Front 51

What is a pyrimidine ring synthesized from?

Back 51

HCO3, NH3, and aspartate

Front 52

What is PRPP an allosteric activator of?

Back 52

carbomoyl phosphate synthase

Front 53

What is the first pyrimidine formed in its biosynthesis pathway?

Back 53

orotate

Front 54

What are the allosteric inhibitors of pyrimidine biosynthesis?

Back 54

UTP and UMP

Front 55

What is the key enzyme in the production of deoxyribonucleotides?

Back 55

ribonucleotide reductase

Front 56

What is used to elute proteins from matrix in ion exchange chromatography?

Back 56

salt

Front 57

Is there more free space in the center of hemoglobin with or without oxygen bound to it?

Back 57

without (relaxed state)

Front 58

What kind of sugar pucker does B-DNA have?

Back 58

C(2') endo

Front 59

What id the difference between monoclonal and polyclonal antibodies?

Back 59

monoclonal bind at 1 site
polyclonal bind at 2 sites

Front 60

What the steps in ELISA?

Back 60

attach antibody
add sample and wash off unbound
add enzyme-linked secondary antibody

Front 61

What are the steps in Western Immunoblotting?

Back 61

SDS-PAGE
transfer to membrane
primary antibody
secondary antibody

Front 62

What are the steps in immunofluorescence microscopy?

Back 62

tissue sample incubated with antibody
wash and add secondary antibody
visualize under microscore

Front 63

What catalyzes the degradation of APP to ABeta peptides in the extracellular fluid?

Back 63

secretase

Front 64

What are three ways to increase reaction rate?

Back 64

raise the temperature
lower the activation energy
break up the reaction into several lower activation energies

Front 65

Is an enzyme's active site generally polar or nonpolar?

Back 65

nonpolar

Front 66

What stabilizes the enzyme-substrate active site?

Back 66

hydrogen bonds
hydrophobic interactions
Van der Waals interactions
ionic interactions

Front 67

What does neuramidase do?

Back 67

cleaves sialic acid residues from flu virus allowing it to be mobile

Front 68

What do cofactors consist of?

Back 68

coenzymes and prosthetic groups

Front 69

What is an apoenzyme?

Back 69

protein part of enzyme minus cofactors of prosthetic groups

Front 70

What does feeback inhibition mean?

Back 70

product inhibits the first enzyme in its pathway

Front 71

What is NAD?

Back 71

coenzyme containing vitamin B3

Front 72

What is FAD?

Back 72

coenzyme containing vitamin B2 and adenosine

Front 73

How does competitive inhibition affect a Lineweaver-Burke plot?

Back 73

Km increases, Vmax doesn't change, increasing [S] reverses the inhibition

Front 74

How does noncompetitive inhibition affect a Lineweaver-Burke plot?

Back 74

Km doesn't change, Vmax decreases, increasing [S] has no affect

Front 75

What are enzymes that catalyze the same reaction called?

Back 75

isoenzymes

Front 76

What is an important example of an isoenzyme?

Back 76

lactate dehydrogenase in heart and muscle