Biochemistry
Protein Folding
Compiled By Simon Mwangi
Edition: 2024/25
, Science | Biochemistry I of V pages
1. What does a sigmoid curve tell us about the mechanism?
That it is cooperative
2. Why do secondary structures happen before tertiary structures?
Because they are closer together
3. What structure does the folding start with?
Primary to secondary
4. What is progressive stabilisation?
You start with interaction of amino acids that are very close and then go on from there so its progressive
5. What is the native structure of a protein?
The active structure which is found in for example the body and is working
6. Where is there more entropy ? in a folded of unfolded protein?
Unfolded because there is more disorder
7. Is there any entropy in the native/folded protein?
Yes but very little as it is very ordered
8. What are the interaction occurring in proteins to form?
Hydrogen bonds, Hydrophobic interaction (most important)Disulphide bonds (second most
9. Can we predict structure folding based on entropy?
If entropy is decreasing then the protein is folding in the right way. If it folds in a wrong way it wont decrease
10. What is the main driving force of protein folding?
That the proteins are emerged in water and therefor have hydrophobic interactions
11. Why are disulphide bonds so important?
Because it makes it more difficult to denature protein with heat
12. What does Leinthals paradox say ?
Mathematically impossible for protein folding to occur by random trying every confirmation until lowest
13. Are there formation of intermediates in protein folding?
Yes
14. When is a reaction favorable, when ^G is positive or negative?
Negative
15. What is chain conformational entropy?
Entropy of the unfolded chain
16. When considering entropy and enthalpy (thermodynamics) which protein is more favoured? Folded or
From a thermodynamic point of view the folded protein is favorable because its ^G is negative
Biochemistry 2024/25 Edition
Protein Folding
Compiled By Simon Mwangi
Edition: 2024/25
, Science | Biochemistry I of V pages
1. What does a sigmoid curve tell us about the mechanism?
That it is cooperative
2. Why do secondary structures happen before tertiary structures?
Because they are closer together
3. What structure does the folding start with?
Primary to secondary
4. What is progressive stabilisation?
You start with interaction of amino acids that are very close and then go on from there so its progressive
5. What is the native structure of a protein?
The active structure which is found in for example the body and is working
6. Where is there more entropy ? in a folded of unfolded protein?
Unfolded because there is more disorder
7. Is there any entropy in the native/folded protein?
Yes but very little as it is very ordered
8. What are the interaction occurring in proteins to form?
Hydrogen bonds, Hydrophobic interaction (most important)Disulphide bonds (second most
9. Can we predict structure folding based on entropy?
If entropy is decreasing then the protein is folding in the right way. If it folds in a wrong way it wont decrease
10. What is the main driving force of protein folding?
That the proteins are emerged in water and therefor have hydrophobic interactions
11. Why are disulphide bonds so important?
Because it makes it more difficult to denature protein with heat
12. What does Leinthals paradox say ?
Mathematically impossible for protein folding to occur by random trying every confirmation until lowest
13. Are there formation of intermediates in protein folding?
Yes
14. When is a reaction favorable, when ^G is positive or negative?
Negative
15. What is chain conformational entropy?
Entropy of the unfolded chain
16. When considering entropy and enthalpy (thermodynamics) which protein is more favoured? Folded or
From a thermodynamic point of view the folded protein is favorable because its ^G is negative
Biochemistry 2024/25 Edition
