Non polar Amino Acids.pptx

in this presentation non polar amino acid with their features and structures are defined .

1. Non- polar aminoacidic

2. Non- polar aminoacid includes: Glycine Alanine Proline Valine Lucine Isoleucine Methionine

3. The molecular structure of NPAA:

4. Glycine The smallest, simplest and lightest amino acid in the body It is the only amino acid that does not have an asymmetric carbon and does not have D and L isomers and does not have optical activity Precursor of purine bases (adenine and guanine), heme, creatine and bile acids and glutathione In the structure of proteins, glycine is mainly found in the β-turn site. Participating in the detoxification of chemical compounds such as benzoic acid, which is added to food as a preservative, and converting it into hippuric acid (high solubility) Along with proline, it is one of the destabilizing amino acids of the alpha helix (-helixα)

5. Alanine As the most abundant amino acid in blood circulation Ammonia transporter from muscles to liver during severe starvation (glucose-alanine cycle) The most compatible amino acid to be placed in the alpha helix of proteins

6. Valine, leucine and Isoleucine They are known as branched chain amino acids. Disturbance in the metabolism of branched amino acids (due to defects in the dehydrogenase enzyme complex) causes maple syrup urine disease (MSUD). Isoleucine has 2 asymmetric carbon atoms

7. Proline Proline is the cyclic form of glutamate. The alpha amine group of proline is of the second amine type, so it is called an imino acid. It has a cyclic structure in the side chain (not aromatic). Incompatible in alpha helix, compatible in β-turn (causes folding in the structure of proteins

8. Methionine Along with ornithine, the precursor of polyamine compounds include spermidine and spermine (polyamines in the cell are attached to anionic molecules such as DNA, which helps to compact them). The active form of methionine (S-adenosylmethionine or SAM), which acts as a methyl group donor in some biochemical reactions This compound has purine in its structure. Methionine is converted to homocysteine ​​by loss of methyl Increasing the concentration of homocysteine ​​in the blood is a risk factor for cardiovascular diseases