As the amino acid chain grows, it folds into a three-dimensional (3-D) structure,
which depends on both the chemical nature and order of the different amino acids.
The 3-D structure determines the function of the protein.
When there is a change in one or more amino acids, then the ability of the protein to function
may be affected. The protein’s function may be unchanged or it may become sluggish,
hyperactive, or inactive.
This delicate folding process is guided by molecular forces such as hydrogen bonding,
hydrophobic interactions, and van der Waals forces. Even minor alterations in temperature,
pH, or sequence can disrupt the folding pattern, leading to misfolded proteins —
a key factor in diseases such as Alzheimer’s or cystic fibrosis.
Understanding protein folding is one of the central goals of modern biochemistry and
molecular biology. It bridges genetics, structural chemistry, and medicine, revealing
how a simple sequence of amino acids transforms into the complex machinery of life.