The following non-polar amino acids are usually found within the hydrophobic core of globular proteins EXCEPT phenylalanine leucine proline The Role of Non-Polar Amino Acids in the Hydrophobic Core of Globular Proteins

Non-Polar Amino Acids’ Role in the Hydrophobic Core for Globular Proteins

The inner core of globular protein globules is often home to non-polar amino acid, also known as the “hydrophobic core”. They are hydrophobic which means they cannot dissolve in water and attract other non-polar molecules. Hydrophobic interactions create a stable force which helps to keep the protein in its globular shape. Research has shown that protein’s hydrophobic core is an important contributor to its overall stability (Kumar and colleagues, 2016; Bhatt and colleagues, 2021). These non-polar amino compounds are typically aromatic, aliphatic or sulfur-containing. Leucine isoleucine methionine tryptophan, phenylalanine, phenylalanine, phenylalanine, phenylalanine, phytylalanine, and methionine are all examples of such amino acids. They form strong hydrophobic interactions between each amino acid and surrounding lipids which help to maintain the protein’s globular shape.
The non-polar amino acid found in the hydrophobic center have also been shown to play a significant role in proper functioning. Cont…