Introduction to Globular and Fibrous Protein
FAQs on Difference Between Globular and Fibrous Protein
1. What is Globular and Fibrous Protein difference?
The main difference between globular and fibrous proteins lies in their structure, solubility, and function. Globular proteins have a compact, three-dimensional structure, are soluble in water, and perform diverse functions such as enzymatic activity, transport, and regulation. In contrast, fibrous proteins have an elongated, thread-like structure, are insoluble in water, and primarily serve structural roles, providing support and strength to tissues. Globular proteins are versatile and soluble, while fibrous proteins are specialized for structural integrity.
2. Are globular proteins involved in enzymatic activity?
Yes, globular proteins are commonly involved in enzymatic activity. Many enzymes, which are catalysts for biochemical reactions, belong to the globular protein class. The three-dimensional structure of globular proteins provides an active site, a region with a specific shape that allows the binding of substrates. This binding facilitates enzymatic reactions, where the globular protein acts as a catalyst, promoting the conversion of substrates into products.
3. Are globular proteins soluble or insoluble?
Globular proteins are soluble in water and other polar solvents. This solubility arises from their three-dimensional structure, which allows them to form hydrogen bonds with water molecules. The hydrophilic amino acid residues on the protein's surface contribute to its solubility. The compact and folded structure of globular proteins helps to shield the hydrophobic amino acids from the surrounding water. Overall, the solubility of globular proteins is crucial for their proper function in biological processes within the aqueous environment of cells.