ex2: chap + fibrous & globular

Question 1

what happens if hsp70 isn’t present when the temp is high

Answer 1

the hydrophobic regions of the unfolded protein will stick to the hydrophobic regions of other proteins and make a mess, causing aggregation + damage to tissue

Question 2

what does hsp70 do

Answer 2

binds to the ho region of an unfolded protein to keep it to itself

Question 3

what are the two parts of hsp60

Answer 3

groes and groel

Question 4

how does groel cavity work

Answer 4

groel cavity is hydrophobic, this attracts the misfolded protein. groes cap goes on and makes cavity be polar. creates good environment for protein to refold.

Question 5

3 characteristics about fibrous proteins

Answer 5

insoluble, simple REPEATING linear strands or sheets (secondary structure), and are structural proteins

Question 6

why are fibrous proteins insoluble

Answer 6

since they are linear, their hydrophobic regions are exposed

Question 7

all fibrous proteins contain 1 type of repetitive _ structure

Answer 7

secondary

Question 8

what is the structure of alpha keratin

Answer 8

coiled coil, 2 alpha helix twisted together

Question 9

what links the structure of alpha keratin

Answer 9

disulfide bonds, they link the helices together

Question 10

how does collagens structure differ from alpha keratins

Answer 10

collagen forms a triple helix (3 alpha helix’s) while alpha helix uses 2 alpha helix to form a coiled coil

Question 11

what bonds tighten collagen

Answer 11

covalent + vdw

Question 12

how many residues per turn does collagen have? what comes after _ residues?

Answer 12

3, gly

Question 13

benefit of having gly in collagen structure?

Answer 13

small = easier to tighten the structure

Question 14

what is lysil oxidase

Answer 14

enzyme that modifies lysine. this allows lysine to form covalent cross link bonds to hold the structure together

Question 15

what is the structure of silk fibroin + bonds that hold it together

Answer 15

b-sheets w vdw = repeating secondary structure

Question 16

whats special about the ala-gly-ala-gly seq in silk fibroin?

Answer 16

interdigitating of ala and gly allows for more contact in the surface areas of each sheet = more vdw bonds = more stability

Question 17

where are the hydrophobic regions of globular proteins?

Answer 17

on the inside

Question 18

what does the structure of globular proteins consist of?

Answer 18

several 2 degree structures = complex 3 degree structure