Non-Polar Amino Acids and the Hydrophobic Core Of Globular Proteins: What Role Does This Play?
These non-polar amino acids can often be found within the inner cores of globular proteins. This is known as their hydrophobic center. Hydrophobic amino acids, which are non-polar, are attracted to 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 often aliphatic or aromatic amino acids. Leucine isoleucine methionine tryptophane, phenylalanine and phenylalanine are all examples of such amino acids. The amino acids have strong hydrophobic interactions that allow them to interact with the surrounding lipids. This helps keep the protein in its original globular form.
Additionally, non-polar amino compounds found within the hydrophobic base have been proven to be a key component of proper protein function. Cont…
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