Polarity of Lysine

Lysine is polar, positively charged and hydrophilic. Lysine is a positively charged polar amino acid. As such, it is the most favoured replacement for another positively charged amino acid (arginine), but it can tolerate replacing other polar amino acids under certain circumstances. Lysine plays an important role in the structure. Firstly, it can be considered somewhat amphiphilic because the part of the side chain closest to the main chain is long, carbon-containing and hydrophobic, while the ends of the side chain are positively charged. For this reason, one can find lysine where the side chain portion is buried and only the charged portion is on the outside of the protein. However, usually lysine prefers the outside of the protein.

Lysines are also often involved in salt bridges, where they pair with negatively charged amino acids (e.g., aspartic acid) to form stable hydrogen bonds, which are important for protein stability.Role of Lysine in Function: Lysines are very common in protein activity or binding sites. Lysine contains a positively charged amino group on its side chain, which is sometimes involved in hydrogen bonding (e.g. anion or carboxylate group) with negatively charged non-protein atoms. Lysine is also frequently modified, particularly by acetylation, which is one of the most common modifications in known proteins.

Application of L-Lysine

Lysine or L-lysine is an essential amino acid, which means it is necessary for good health, but the body cannot make it. Lysine must be obtained from food or supplements. Lysine can be used for calcium intake. Lysine is used in people with osteoporosis to improve the ability of our intestines to absorb calcium. Because calcium is essential for maintaining healthy bones, taking lysine is ideal for making the most of your calcium supplements. Lysine is also important for normal growth and plays a vital role in the production of carnitine, a nutrient responsible for converting fatty acids into energy and helping to lower cholesterol.