amino acids and proteins

Question 1

nonpolar aliphatic AA

Answer 1

glycine alanine valine leucine isoleucine methionine

Question 2

aromatic

Answer 2

phenylalanine tyrosine tryptophan

Question 3

polar and uncharged

Answer 3

serine proline threonine cytosine asparagine glutamine

Question 4

polar and positive

Answer 4

histidine arginine lysine

Question 5

polar and negative

Answer 5

aspartate and glutamate

Question 6

example of a molecule that uses disulfide bridges

Answer 6

insulin

Question 7

scurvy is when you screw up what modification of what amino acid

Answer 7

vitamin c needed to turn proline into hydroxyproline

Question 8

who cares about carboxylated glutamine and what does it need and what drug helps when this is fucked up

Answer 8

vitamin k- important for clotting- warfarin (aka coumadin)

Question 9

force of H bonds

Answer 9

1-7 kj/mol

Question 10

alpha helix is how many residues per turn and how many angstroms

Answer 10

3.6 r/t and 5.4 angstroms

Question 11

what do you get when your glycosylation pathways are genetically fucked up

Answer 11

congenital disorder of glycosylation

Question 12

what is gleevec and who uses it

Answer 12

tyrosine kinase inhibitor used to treat CML

Question 13

what is bortezomib and why do we use it

Answer 13

protease inhibitor to treat multiple myeloma

Question 14

3 covalent bonds in peptide backround- which is phi, which is psi, and which has double bond character

Answer 14

1. Ca- carbonyl of AA1 (psi), 2. Carbonyl C of AA1- amide N of AA2 (double bond character, phi), 3. aminde N and Ca of AA2

Question 15

what determines secondary structure

Answer 15

H bonding between amide N and carbonyl oxygen

Question 16

what is the 2ndary structure of collagen

Answer 16

triple L handed helix

Question 17

in the alpha helix, which AAs H bond to each other and which are on top of each other

Answer 17

N bonds to N+4, 1st and 8th are stacked

Question 18

what 2 AAs can’t form alpha helices

Answer 18

glycine and proline

Question 19

hemoglobin is mostly what 2ndary structure

Answer 19

alpha helix

Question 20

thalassemia is caused by what defect in secondary structure

Answer 20

unstable alpha helices in hemoglobin

Question 21

give an example of a protein thats mostly beta sheets

Answer 21

immunoglobulin

Question 22

how do you monitor a proteins secondary structure

Answer 22

circular dichroism

Question 23

2 major types of tertiary structures

Answer 23

fibrous and globular

Question 24

fibrous proteins tend to have what unique characteristic regarding their 2ndary strucure

Answer 24

EITHER alpha or beta- not mixed

Question 25

what is the role and solubility of fibrous proteins

Answer 25

insoluble, strucural/protetive

Question 26

most proteins in the body have what tertiary structure

Answer 26

globular

Question 27

globular proteins solubility?

Answer 27

water or lipid soluble

Question 28

what are the most frequently found AAs in turns and loops

Answer 28

glycine and proline

Question 29

how many polypeptides are in hemoglobin

Answer 29

4

Question 30

what does Kd represent

Answer 30

disassociation constant aka binding strength of a protein and ligand

Question 31

what are the 2 states of hemoglobin

Answer 31

tense and relaxed

Question 32

2 major ways to determine protein structure

Answer 32

crystallography--> Xray diffraction and NMR usig magnetic resonance

Question 33

what protein can totally refold on its own specifically

Answer 33

ribonuclease A

Question 34

two major classes of chaperones

Answer 34

Hsp70 and GroEL

Question 35

what does protein disulfide isomerase do

Answer 35

catalyzes the exchange between free cysteines and disulfide bonds to make the right disulfide bonds

Question 36

prolyl isomerase does what

Answer 36

catalyzes the conversation between trans and cis proline

Question 37

prion disease means changing from ___ secondary structure to ___

Answer 37

alpha helix-- beta sheet

Question 38

3 major protein purification approaches

Answer 38

gel filtration chromatography (sep based on size), ion exchange chromatography( separates based on charge differences) affinity chromatography (utilizes proteins affinity to bind certain ligands)

Question 39

how do you determine the mass of a protein

Answer 39

mass spectrometry

Question 40

what does Edman degradation do

Answer 40

determines the N terminal sequence of a protein