How Protein folds? During translation, the linear chain of amino acids formed will be gradually released from the ribosome, and these amino acids should fold properly to make a functional protein, the ultimate nano machines in the cells. Protein folding is undoubtedly the most critical events that determine the ability of that given protein to work properly.
How protein folds? Is it a random process? It shouldn’t be, as folding determines the function.
- Protein folding refers to the set of ordered pathways by which protein folds into their native functional confirmation.
- Protein folding is primarily driven by hydrophobic forces.
- The first insight to this question was provided by Christian Anfinsen at the NIH. He was working on the properties of ribonuclease A (a single chain protein of 124 amino acids with 4 di-sulphide bonds). He unfolded (denatured) ribonuclease A using urea and mercaptoethanol (denaturants). The protein lost its function. Then he allowed to renature ribonuclease A by removing denaturants, and found out that ribonuclease A folded spontaneously and become functional. He concluded that Ribonuclease A can self assemble into its 3D functional structure.
- Primary structure dictates the 3D structure of protein Or primary structure has the program or code for forming a properly folded functional protein.
Protein Folding inside the Cell
- Inside the cell, protein folding is assisted by different proteins collectively called as accessory proteins.
- Protein folding assisting proteins or accessory proteins.
The importance of studying protein folding?
- to engineer novel protein
- to get better insight into diseases associated with protein folding