Why Do Physical Processes Favor Entropy Maximization Over Energy Minimization?

Click For Summary
SUMMARY

The discussion centers on the principles of thermodynamics, specifically the second law which dictates that physical processes favor entropy maximization rather than energy minimization. Gibbs Free Energy (ΔG) is crucial for determining the direction of these processes, as it incorporates temperature effects that influence reaction spontaneity. The conversation also touches on the relationship between protein folding and entropy, questioning whether folding increases or decreases entropy, and clarifying the distinction between enthalpy and free energy in biochemical systems.

PREREQUISITES
  • Understanding of the second law of thermodynamics
  • Knowledge of Gibbs Free Energy (ΔG) and its formula
  • Familiarity with protein structure and folding dynamics
  • Basic concepts of enthalpy in biochemical systems
NEXT STEPS
  • Research the relationship between temperature and Gibbs Free Energy in biochemical reactions
  • Explore the implications of protein folding on entropy and thermodynamics
  • Study the differences between enthalpy and free energy in detail
  • Investigate the applications of the second law of thermodynamics in biological systems
USEFUL FOR

This discussion is beneficial for students and professionals in biochemistry, thermodynamics, and molecular biology, particularly those interested in the thermodynamic principles governing biochemical processes and protein dynamics.

mather
Messages
146
Reaction score
0
hello!

there is no law that says that processes occur physically towards the energy minimization of the system

however, there is a law (second thermodynamic) that says that processes occur physically towards the entropy maximization

1) so, why do we need ΔG (Gibbs free energy) to predetermine a process' direction?

2) also, why ΔG is depended to temperature?

3) I have seen in a tutorial where they said that moving from primary to secondary and to tertiary etc, protein structure, it is a increases in protein's entropy! in a textbook, I read the opposite (which is more correct imo, since a folded protein has some fixed substructures, thus the number of possible structures is limited)
which is the correct? and if folding decreases its entropy, how is this thermodynamically compliant?

4) what is the difference of enthalpy and free energy of a biochemical system?

thanks!
 
Last edited:
Physics news on Phys.org
1) Gibbs Free Energy is a thermodynamic potential which determines the non-PV work or "useful" work in initiating and proceeding a process.

2.) Check the formula for Gibbs Free Energy. Usually, at higher temperatures, processes proceed more easily, even the non-spontaneous, difficult to get products can be formed.
 

Similar threads

  • · Replies 4 ·
Replies
4
Views
4K
  • · Replies 12 ·
Replies
12
Views
3K
  • · Replies 11 ·
Replies
11
Views
3K
Replies
10
Views
4K
  • · Replies 13 ·
Replies
13
Views
4K
  • · Replies 4 ·
Replies
4
Views
1K
  • · Replies 6 ·
Replies
6
Views
3K
  • · Replies 22 ·
Replies
22
Views
6K
  • · Replies 1 ·
Replies
1
Views
2K
  • · Replies 10 ·
Replies
10
Views
3K