Biochemistry

Question 1

What are two important biochemical reactions?

Answer 1

Acid-base rxns and Redox reactions

Question 2

What are the cofactors?

Answer 2

Metals and coenzymes (Vitamins)

Question 3

What is an apoenzyme?

Answer 3

An enzyme without its cofactor

Question 4

What is a holoenzyme?

Answer 4

An enzyme with its cofactor

Question 5

What are the metal cofactors?

Answer 5

Zn, Mg, Cu, Fe

Question 6

What occurs in a lyase reaction?

Answer 6

Forms a double bond

Question 7

What occurs in a double displacement reaction?

Answer 7

A product is released before a second substrate binds

Question 8

What regulates ATCase and what is this an example of?

Answer 8

CTP, negative allosteric inhibitor

Question 9

What is the alternative conformation sequence?

Answer 9

VDLLKN

Question 10

What are the 2 beta sheet structural forms?

Answer 10

Parallel - 1 amino acid

Antiparallel - 2 amino acids

Question 11

What does O2 bind on Hb?

Answer 11

E7 Distal Histidine

Question 12

Where is Fe2+ located on the heme group?

Answer 12

F8 Proximal Histidine

Question 13

What the difference between secondary and tertiary structures?

Answer 13

Secondary are alpha helices and beta sheets, tertiary contains S-S bonds, hydrophobic interactions, H-bonds, metal ions

Question 14

Collagen is a ______ protein with what structure?

Answer 14

triple helix; fibrous (pro-gly)

Question 15

What an example of a globular protein?

Answer 15

Hb, albumin

Question 16

Types of bonds in bovine?

Answer 16

ABC method = cooperative; 1 intra- and 2 intersulfide bonds

Question 17

Urea breaks what bonds?

Answer 17

H-bonds; secondary structure

Question 18

Ethanol breaks what bonds?

Answer 18

Disulfide bonds; tertiary structure

Question 19

Molten globule is primarily which folding sequence?

Answer 19

Secondary; contains a larger radius

Question 20

What’s an example of a motif?

Answer 20

Calmodulin

Question 21

What an example of a metamorphic/alternate conformation molecule?

Answer 21

Lymphotactin (Chemokine and GAGs)

Question 22

A high score tells us what about hydrophobicity?

Answer 22

More hydrophobic

Question 23

What are the denature chemicals? (DOC)

Answer 23

Detergents = SDS
Organics = OH, TCO
Chaotropic = Urea (reducing agent), Guanidine Hydrochloride

Question 24

What are the methods for analyzing proteins? (FCTUB)

Answer 24

Fluorescent
Circular dichroism (+,-)
Turbidity
UV - aromatics 180nm
Biological activity

Question 25

What are accessory proteins?

Answer 25

Chaperones = PDI - disulfide bonds

PPI - cis/trans

Question 26

What are the molecular chaperones?

Answer 26

Chaperonins

HSP

Question 27

3 steps to forming amyloid plaques?

Answer 27

San Fran Deposits

Seeding
Fibrillation
Deposit

Question 28

What are the heavy metals?

Answer 28

Cd, Pb, Hg

Question 29

the 2 classes of metalloproteins?

Answer 29

Transfer/storage and Enzymes

Question 30

What are the types of enzyme metalloproteins? (3)

Answer 30

Electron carriers, metal and oxygen management

Question 31

What can infectious proteins turn into?

Answer 31

Amyloid plaques (beta)
Prions

Question 32

What are the covalent modifications of amyloid fibrillation in neurodegenerative diseases? (SUMOPrPO)

Answer 32

Sumoylation
Phosphorylation
Oxidation
Proteolytic cleavage

Question 33

What’s the portion for heme binding on Hb?

Answer 33

EFG (entire heme is A-H)

Question 34

What are the 3 enzymes in the catalytic triad?

Answer 34

His 57
Asp 120
Ser 195

These are the active sites of Chymotrypsin

Question 35

Which zymogen exists in the stomach?

Answer 35

Pepsinogen

Question 36

What’s the enzyme that cleaves and activates zymogens in the stomach and pancreas?

Answer 36

Enteropeptidase

Question 37

What bonds are in the phi torsion?

Answer 37

C-N

Question 38

What bonds are in the psi torsion?

Answer 38

C-C

Question 39

What are the folding metals?

Answer 39

Ca2+, Mg2+, Fe2+, Cu2+