Non polar Amino Acids.pptx
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This document summarizes the properties of 7 non-polar amino acids: glycine, alanine, proline, valine, leucine, isoleucine, and methionine. It describes their molecular structures, roles in proteins and metabolic pathways. Glycine is the smallest amino acid and participates in purine synthesis. Alanine transports ammonia from muscles to liver. Valine, leucine and isoleucine are branched chain amino acids, and their metabolism defects cause maple syrup urine disease. Proline has a cyclic side chain and causes protein folding. Methionine donates methyl groups and its metabolism impacts cardiovascular health.
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PROTEIN AND AMINO ACIDS-CLASS-I.pptx
There are 20 amino acids that are the building blocks of proteins. Amino acids are classified based on their polarity and the nature of their side chains. They can be hydrophobic, hydrophilic neutral, acidic, or basic. Proteins are polymers of amino acids joined by peptide bonds. They have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. Denaturation disrupts a protein's structure leading to loss of biological activity.
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Amino acids can be classified in several ways:
1. Based on their source as either standard/primary amino acids that are incorporated into proteins or non-standard amino acids that do not participate in protein synthesis.
2. By the properties of their side chains as non-polar, polar uncharged, acidic, or basic. Non-polar amino acids cluster inside proteins while polar ones interact through hydrogen bonding.
3. According to their roles in metabolism as either glycogenic, ketogenic, or both glycogenic and ketogenic.
Selenocysteine, containing the element selenium, is now recognized as the 21st standard amino acid despite being incorporated via a unique genetic mechanism during translation.
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1) Amino acids can be classified based on their source, side chain structure, amphoteric properties, nutritional requirements, and metabolic fate. 2) The 20 standard amino acids are incorporated into proteins during translation based on codon sequences, while non-standard amino acids play other important biological roles. 3) Selenocysteine is the 21st amino acid encoded by UGA codons when accompanied by a selenocysteine insertion sequence in mRNA.
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This document discusses amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, which includes an amino group, carboxyl group, and side chain. The document then classifies amino acids according to their side chains and discusses their optical, acid-base, and buffer properties. It also distinguishes between standard and non-standard amino acids, and essential vs non-essential amino acids which must be obtained through diet.
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- At physiological pH, the carboxyl group is dissociated forming a negatively charged carboxylate ion and the amino group is protonated.
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Protein.pptx
Proteins are composed of chains of amino acids and perform essential functions in the body. There are 20 standard amino acids, some of which are essential and must be obtained through diet. Amino acids link together through peptide bonds to form polypeptide chains or proteins. Proteins have four levels of structure and take on complex shapes that enable their many functions like structure, movement, hormones, and enzymes. A deficiency or excess of proteins can cause health issues.
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Amino acids are the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain. There are 22 protein amino acids that are polymerized to form proteins, which carry out important structural and functional roles in the body. Amino acids can also be classified based on their chemical properties and metabolic fates. The peptide bond forms when amino acids condense, linking them together into polypeptides and proteins.
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PROTEIN AND AMINO ACIDS-CLASS-I.pptx
There are 20 amino acids that are the building blocks of proteins. Amino acids are classified based on their polarity and the nature of their side chains. They can be hydrophobic, hydrophilic neutral, acidic, or basic. Proteins are polymers of amino acids joined by peptide bonds. They have primary, secondary, tertiary, and quaternary levels of structure that determine their shape and function. Denaturation disrupts a protein's structure leading to loss of biological activity.
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3. According to their roles in metabolism as either glycogenic, ketogenic, or both glycogenic and ketogenic.
Selenocysteine, containing the element selenium, is now recognized as the 21st standard amino acid despite being incorporated via a unique genetic mechanism during translation.
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Proteins are composed of chains of amino acids and perform essential functions in the body. There are 20 standard amino acids, some of which are essential and must be obtained through diet. Amino acids link together through peptide bonds to form polypeptide chains or proteins. Proteins have four levels of structure and take on complex shapes that enable their many functions like structure, movement, hormones, and enzymes. A deficiency or excess of proteins can cause health issues.
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1. Amino acids are obtained from digestion of dietary proteins, breakdown of body proteins, endogenous synthesis, and are used for synthesis of body proteins, non-protein specialized products, and as an energy source.
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- There are 20 standard amino acids that vary in properties based on their side chains. Phenylalanine, methionine, and tryptophan are hydrophobic while cysteine forms disulfide bridges.
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- 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 valine Lucine Isoleucine
- 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