Midterm

Question 1

properties of protein structure

Answer 1

size
shape
charge
hydrophobic/hydrophillic

Question 2

prosthetic group

Answer 2

a molecules that is permanently associated with a protein and required for its function

Question 3

ligand

Answer 3

a molecule that is bound reversibly by a protein

Question 4

binding site

Answer 4

the region a protein surface that interacts with a ligand

Question 5

induced fit

Answer 5

structural adaptation b/w protein and ligand

Question 6

substrates

Answer 6

are ligands that are chemically altered by the protein (enzyme) they bind

Question 7

catalytic/active site

Answer 7

site on the enzyme where the substrate binds and chemical transformation occurs

Question 8

myoglobin

Answer 8

monomer binds and stores O2 in muscle

Question 9

hemaglobin

Answer 9

blood protein binds reversibly to oxygen

• O2 transporter
• tetramer

Question 10

leghemoglobin

Answer 10

protects bacteria from O2 so it can make N

-found in legumious plants

Question 11

the subunits of hemoglobin are held together by?

Answer 11

1, hydrophobic interactions

2. hydrogen bonds
3. ion pairs (salt bridges)

Question 12

kinase

Answer 12

take some molecule X-OH using ATP as a source of phosphate you make your X a phosphate group

Question 13

phosphatase

Answer 13

• undoes the work of kinase but doesn’t do the reverse reaction
• cleaves it using water not a reverse reaction b/c you don’t get ATP back
• hydrolyses phosphate groups

Question 14

phosphorylase

Answer 14

use something other than water to remove a phosphate group

Question 15

hydrolase

Answer 15

break any sort of ether type bond by using water

Question 16

allosteric enzyme

Answer 16

a regulatory enzyme with catalytic activity modulated by the noncovalent binding of a specific compound at a site other than the active site

Question 17

phosphoryl groups introduce…

Answer 17

1. a relatively bulky group
2. charge
3. hydrogen bonds
4. site for protein-protein interactions

Question 18

important promoters of clotting

Answer 18

• vit K
• Ca2+
• thrombin
• factor XIIIa

Question 19

Order of events in the ATCase reaction

Answer 19

1. Carbamoyl phosphate (CP) binds the active site
2. Asp then binds the active site, this leads to large changes in quaternary structure
3. condensation reaction
4. the product N-carbamoyl-L asp (CA) is released first
5. Pi is released last

Question 20

Phenylalanine

Answer 20

Phe, F

very non-polar (hydrophobic)

Question 21

Alanine

Answer 21

Ala, A

very non-polar (hydrophobic)

Question 22

Valine

Answer 22

Val V

very non-polar (hydrophobic)

Question 23

Isolucine

Answer 23

Ile I

very non-polar (hydrophobic)

Question 24

Leucine

Answer 24

Leu L

very non-polar (hydrophobic)

Question 25

Methionine

Answer 25

Met M | very non-polar (hydrophobic)

Question 26

Cysteine

Answer 26

Cys C | moderately non-polar (hydrophobic)

Question 27

Glycine

Answer 27

GLy G | moderately non-polar (hydrophobic)

Question 28

Proline

Answer 28

Pro P | moderately non-polar (hydrophobic)

Question 29

Tryptophan

Answer 29

Trp W | moderately non-polar (hydrophobic)

Question 30

Tyrosine

Answer 30

Tyr Y | moderately non-polar (hydrophobic)

Question 31

Glutamine

Answer 31

``` Gln Q polar uncharged (hydrophillic) ```

Question 32

Asparagine

Answer 32

``` Asn N polar uncharged (hydrophillic) ```

Question 33

Serine

Answer 33

``` Ser S polar uncharged (hydrophillic) ```

Question 34

Threonine

Answer 34

``` Thr T polar uncharged (hydrophillic) ```

Question 35

Lysine

Answer 35

Lys K | polar positively charged (hydrophillic)

Question 36

Histidine

Answer 36

His H | very polar + charge (hydrophillic)

Question 37

Arginine

Answer 37

Arg R | polar + charge (hydrophillic)

Question 38

Glutamate

Answer 38

Glu E | very polar - charge (hydrophillic)

Question 39

Aspartate

Answer 39

Asp D | Polar - charge (hydrophillic)