Top Posters
Since Sunday
e
5
R
5
e
4
4
d
4
o
3
p
3
t
3
3
m
3
p
3
m
3
SlideshowReport

Contributions to the free energy of folding of globular proteins

Description
The conformational entropy change works against folding, but the enthalpy of internal interactions and the entropy change from the hydrophobic effect favor folding.

Summing these three quantities makes the total free energy of folding negative (favorable); thus, the folded structure is stable.
Related Images
Add Comment
Explore
Post your homework questions and get free online help from our incredible volunteers
  999 People Browsing
Your Opinion
Who's your favorite biologist?
Votes: 587