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. They are hydrophobic which means they cannot dissolve in water and attract other non-polar molecules. The protein is kept in its original globular form by this hydrophobic interaction. The hydrophobic center of the protein has been shown to be a key contributor to protein stability in studies (Kumar, 2016; Bhatt, 2021). Non-polar amino acid found within the hydrophobic center are usually aliphatic and aromatic, as well as sulfur-containing. These amino acids are leucine and isoleucine as well as phenylalanine (methionine), phenylalanine (methionine), tryptophan, cysteine, and phenylalanine. 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…
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