Insulin is a globular protein and a good structure to analyse for the folding of globularproteins. Why is this the case

Insulin is a good structure to analyze for the folding of globular proteins for several reasons:

1. Size: Insulin is relatively small for a protein, with only 51 amino acids. This makes it easier to study than larger, more complex proteins.

2. Structure: Insulin is a globular protein, which means it folds into a compact, spherical shape. This is a common structure for proteins, so studying insulin can provide insights into how other proteins fold.

3. Disulfide Bonds: Insulin has three disulfide bonds, which play a crucial role in its folding. Studying these bonds in insulin can help scientists understand the role of disulfide bonds in protein folding more generally.

4. Medical Relevance: Insulin is medically important because it regulates blood sugar levels. Misfolded insulin can lead to diseases like diabetes, so understanding how insulin folds correctly can have important medical implications.

5. Availability of Data: There is a lot of data available on insulin, including its sequence, structure, and function. This makes it easier to study than proteins that are less well-characterized.