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Protein Folding - Anfinsen's Experiment
- 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.
- Inside the cell, protein folding is assisted by different proteins collectively called as accessory proteins.
- Protein folding assisting proteins or accessory proteins .
- to engineer novel protein
- to get better insight into diseases associated with protein folding
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