The Energetics of Protein Folding Flashcards
Are proteins stable? How stable?
Yes, otherwise they wouldn’t form.
Not very stable, proteins, have not evolved to be optimally stable, they have evolved to be optimally functional.
Are larger proteins, usually more stable than smaller proteins?
No, proteins are often modular, in other words folded into multiple domains making size unimportant for stability usually.
What are the four main factors stabilizing the native state of proteins? Explain the factors. (Keep in mind that one has to consider the folded versus unfolded state in water.)
Test:
True or false: denaturation is usually not reversible.
False! It often is reversible.
True or false: Breaking SS bridges is not required for denaturation.
True! But it is required to arrive at a true random coil.
What are three popular denaturants?
What determines the structure of a protein?
The primary sequence of amino acids.
Describe the current theory on folding pathways to reach the native state.
What are the two types of motion that occur with proteins?
Explain confirmational change in proteins from functional motions.
Example: Calmodulin: this is a calcium signal transducer. It detects, calcium, and then undergoes a confirmational change.
This change requires both calcium and target peptide.
Explain thermal motion of proteins.
