PPT-GLUCOGENIC & KETOGENIC AMINO ACIDS

DR AMINA BIOCHEMISTRY All tissues have some capability for synthesis of The nonessential amino acids Amino acid remodeling and Conversion of nonamino acid carbon skeletons into amino acids and other derivatives that contain nitrogen . What are amino acids?. Amino acids are the building blocks of proteins.. In the body, they exist as zwitterions.. Zwitterions can behave as both an acid or a base.. Today we will:. Study . the acid-base properties of amino acids, . C483 Spring 2013. Questions. 1. . Amino acids with non-. ionizable. side chains are zwitterions when they are ________.. A. ) in any solution . . D) in alkaline solutions only . B. ) at physiological pH, pH = 7.4 . (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.. 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.. Stryer. Short Course. Chapter . 3. Amino Acid Structure. Alpha carbon. Sidechain. Proteins. peptides. Stereochemisty. L-amino acids. Glycine. R/S . vs. D/L. L-isoleucine. racemization. Ionization of Amino Acids. 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.. 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). 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: . Richard D. Howells, PhD. Dental Biochemistry Lecture 24. 2. Learning Objectives. To describe the urea cycle and its fundamental role in the excretion of nitrogen.. To . distinguish between . glucogenic. 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 . backbone.  . atoms . (see aminoAcids1).  but a unique set of . side chain . atoms. It's the side chains that make the 20 amino acids different from each other. . 1. Use the three identical backbone pieces and three unique side chain pieces below to construct three amino acids in the space to the right.. u. sing paper chromatography. Kate Andrews. Lorraine Bruce. Unit 1 DNA and the Genome. 3 Control of gene expression. Separation and identification of amino acids using paper chromatography.. Cells and Proteins. 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.