PPT-Amino Acids Do Now : Draw an

amine group Draw a carboxylic acid group Join them together to form a molecule with an amine and a carboxylic acid group Amino Acids Building blocks of proteins Two functional groups a carboxylic acid and a primary amine. (Foundation Block). Dr. Ahmed Mujamammi. Dr. . Sumbul. . Fatma. Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. Codons. Prefixes, Suffixes and Vocabulary. Poly. = many. Peptide bond . =bond between two amino acids.. Anti. = against, opposite. Dehydration. = loss of water. Polypeptide. = long assembled string of amino acids.. CHAPTER 3, Part 1 . Amino Acids and Peptides . To know the structure and naming of all 20 protein amino acids. To know the structure and properties of peptides and the particularly the structure of the peptide bond.. Subunits (building blocks) of peptides and proteins. Neurotransmitters. Metabolic intermediates. glutamate. γ. -. aminobutyric. acid. (GABA). Proteins are synthesized from 20 ‘standard’ . α. -amino acids. Their names have 3- and 1-letter abbreviations.. (Foundation Block). Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. Non-standard amino acids.. Derivatives of amino acids.. 18. /2014. Biochemistry I. Dr. Loren Williams. Proteinogenic Amino Acids. An amino acid contains . an amine group . a carboxylic acid group, . a side-chain (or R-group,. all attached to the same chiral carbon atom (the Cα). DR AMINA . BIOCHEMISTRY. All tissues have some capability for synthesis of:. The non-essential amino acids,. Amino acid remodeling, . and Conversion of non-amino acid carbon skeletons into amino acids and other derivatives that contain nitrogen. . Part 1 - Amino Acids. Structure and Chemistry. Building Blocks of Proteins. Essential Amino Acids. Basic Structure. Stereochemistry. Side Chain Chemistry. Properties. Ionization. Bonding. Amino Acids & Proteins. UNIT IV:. Nitrogen Metabolism. Part 2. Most of the nitrogen in the diet is consumed in the form of protein, typically amounting to 70–100 g/day in the American diet . Proteins are generally too large to be absorbed by the intestine. . 1. . Overview. The catabolism of the amino acids involves:. Removal of α-amino groups. . Breakdown of the resulting carbon skeletons.. The resulting compounds will be used to form seven intermediate products: . Amino acids are weak . polyprotic. acids . . Neutral amino acids are (. gly. , ala, threonine ) are treated as diprotic acids .. acidic amino acids (. glu. , asp,) are treated as . triprotic. acids .. Peptide bond formation. : . α-carboxyl group of one amino acid (with side chain R1) forms a covalent peptide bond with α-amino group of another amino acid . ( . with the side chain R2) by removal of a molecule of water. The result is : Dipeptide ( i.e. Two amino acids linked by one peptide bond). By the same way, the dipeptide can then forms a second peptide bond with a third amino acid (with side chain R3) to give . imino. acid.” . Figure 5: Comparison of the secondary amino group found in proline with the primary amino group found in other amino acids such as alanine.. 2. Proline: . Proline differs from other amino acids in that its side chain and amino N form a rigid, five -member red ring structure (Figure 5). Proline, then, has a secondary (rather than a primary) amino group. It is frequently referred to as an “. BSc 3. rd. year . AMINO ACIDS. C. lassification of amino acids . Classification according to nature of side chain. PREPARATION OF AMINO ACIDS. 1. Gabriel Phthalimide synthesis. 2. Strecker’s synthesis.