9. The main force involved in protein folding are-

   (1) H-bonding
   (2) Hydrophobic interactions
   (3) Covalent bonds
   (4) Vander wall force

   What is the Main Force Involved in Protein Folding?

What is the primary force behind the folding of proteins?

The highly ordered process of protein folding establishes a protein’s three-dimensional structure. Various molecular forces help to stabilise this structure, which is essential for biological function.

Hydrophobic Interactions (Option 2) is the right response.

Hydrophobic interactions are the main factor causing protein folding among the options provided because:

In order to avoid water, hydrophobic (non-polar) amino acids have a tendency to group together inside proteins.

This lowers the energy of the system by minimising the breaking of hydrogen bonds in the nearby water.

By exposing hydrophilic residues to the aqueous environment and burying hydrophobic residues, proteins attain a stable conformation.

The Reasons Other Choices Are Secondary

Option 1: Hydrogen Bonding

Alpha-helices and beta-sheets are examples of secondary structures that are stabilised by hydrogen bonds

Covalent Connections (Choice 3):

Disulphide bonds between cysteine residues are an example of a covalent bond that adds stability but does not initiate folding.

Forces of Van der Waals (Option 4):

Although they don’t have a major impact on folding, these weak interactions aid in maintaining protein structure.

Conclusion: Protein Folding Is Driven by Hydrophobic Interactions

Option 2 is the right response because hydrophobic interactions are the main mechanism by which proteins fold into their functional structures. These forces are essential for preserving cellular functions, enzyme activity, and protein stability.