Protein function, myoglibin, hemoglobin

Question 1

What makes Keratin a very good example of a quatrenary structure

Answer 1

1. has tensile strength, forms strong base with leucines, has backbone H bonds and good placement of side chains

Question 2

What are globins made of

Answer 2

Alpha helixes

Question 3

What do all globins have structurally

Answer 3

heme ring that holds the molecules together

Question 4

What is in the center of heme

Answer 4

iron

Question 5

Where are hemoglobin and myoglbin identical vs different

Answer 5

at a tertiary level, they are identical. The only difference is at a quartenary structure- folded proteins come together to form larger proteins.
Myoglobin does not bind to anything else
hemoglobin is a tetromer, have 4 bound together

• Look the same when one on one, but hemoglobin has 4. Has to live as tetromer or won’t fold properly

Question 6

How much oxygen can hemoglobin vs myoglibin carry

Answer 6

Hemoglobin: 4 times as much as myoglobin

Question 7

In high oygen, is myoglibin binding or releaseing oxygen

Answer 7

binding- myoglobin tightly binds until around 10% O2. As we approach 0, let go of O2

Question 8

T state vs R state

Answer 8

-T: pulling on everything and stretching middle part of protein, cause tension (T)
-R: collapsed hole in middle, relaxed (R).
-Binding oxygen usually causes relaxation because makes less tense

Question 9

What type of interaction forms between a positive and negative in a protein

Answer 9

A salt bridge

Question 10

What is end terminus of proteins

Answer 10

C terminus- negatively charged- natural state is moving, not super still.

Question 11

What charge is lysine

Answer 11

positive

Question 12

What does 2,3,-BPG do

Answer 12

Negatively charged, form bonds with other things
In tissues, most prevalant molecule in blood
- Fit in T state, stabilize, allow for hemoglobin to dump oxygen,