Protein folding and Thermodynamics Flashcards
Anfinsen’s experiment
- Unfolded proteins are inactive ∴ Structure ➝ Activity. 2. Correct disulphide bond formation occurs after folding. 3. All the information for a protein to fold correctly is
contained in the amino acid sequence. - Disulphide bonds stabilise folded proteins.
What directs protein folding
The different types of bonds or interactions make different contributions to protein folding, they have different strengths, directional properties and roles in folding
Thermodynamics
The alteration of the content of energy and its distribution that take place when a system passes from an initial, defined state into a terminal state @equilibrium
∆X - the change in X
changed in temp ∆X is defined as ∆T= Tfinal - Tinitial
Can be applied to chemical or physical changes
Laws of themodynamics
1.Energy can never be created or destroyed
If the energy of a system changes the energy must be transferred to another system
∆U= q+w q=heat w=work
Enthalpy
∆U=q+w
at constant pressure q=∆U (change in enthalpy)
If heat is released the system has a decrease in enthalpy (∆H<0) and is exothermic
If heat is absorbed the system has an increase in enthalpy (∆H>0) and is endothermic
STANDARD
Pressure 10^5 Pa
Concentration of 1M
Hess’s law
The overall enthalpy change for any process is constant, regardless of how the reaction is carried out
Entropy
Amount of disorder
∆rS= Sproducts - Sreactants
J mol-1 K-1
ANY EVENT THAT IS ACCOMPANIED BY AN INCREASE IN THE ENTROPY OF THE SYSTEM HAS A TENDENCY TO OCCUR SPONTANEOUSLY
Gibbs energy (G)
Entropy change of the universe: ∆Stotal= ∆Ssystem +∆Ssurroundings
∆Stotal= ∆Ssystem - ∆Hsystem
T
G=H-TS
A process is spontaneous when ∆G<0 at constant p and T
protein folding the free energy change associated
DGtotal = DHchain+ DHsolvent - T DSchain -T DSsolvent