B2.045 Prework 2 Cooperativity and Allostery Flashcards Preview

MCM Test 3 > B2.045 Prework 2 Cooperativity and Allostery > Flashcards

Flashcards in B2.045 Prework 2 Cooperativity and Allostery Deck (10)
Loading flashcards...
1

what is the difference between allosteric and cooperative binding?

cooperative- same binding site, same ligand
allosteric- different binding site, different ligand

2

how is allostery seen on an enzyme curve?

shift in Kd

3

what are two types of allostery?

inhibitory allostery- initial substrate diminishes binding of second substrate
enhancing allostery- initial substrate enhances binding of second substrate

4

why does nature need allostery?

regulation
regulation
regulation

5

what are two examples of cooperativity?

homo-oligomers- binding site is repeated on each subunit
single polypeptide chain with identical binding sites

6

how can you visualize cooperativity on an enzyme curve?

steeper sigmoidal curve; midpoint is weighted average of a site with low affinity and a site with high affinity

7

what is the hallmark of negative cooperativity?

never reaches 100% bound

8

how is positive cooperativity used in nature?

response range to ligand change narrows, aka once a little binds, a lot more can bind
similar to an on/off

9

how is negative cooperativity used in nature?

changes at higher ligand concentrations do not affect protein function
constant protein function across a wide range of ligand concentrations

10

what are some possible advantages of allosteric drugs?

more subtle effects, potential to ramp up function or slow it rather than on/off
expands the number of search targets