PPT-Polypeptides, Amino Acids, and

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. 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.. Essential idea: Proteins have a very wide range of functions in living organisms.. One of the central ideas in Biology is that structure dictates function. Above you can see insulin in its secondary, tertiary and quaternary structures. Polypeptides vary hugely in the combination and number of amino acids that they are composed from. Even if we consider a single polypeptide it's properties, and hence it's function, would vary greatly depending on it's level of structure. Insulin can exist in all these forms, but the active form, which controls blood glucose levels, is a the tertiary structure.. https://www.youtube.com/watch?v=hpaki7F4HR0. http. ://www.wisc-online.com/objects/index_tj.asp?objID=AP13304. Cells contain thousands of different proteins, each performing a specific task.. Examples: Enzymes, . 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. 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: . Polypeptides . are chains of amino acids linked together by condensation reactions. the main, or only, component in proteins. Some proteins are composed of only one polypeptide chain, while others are made of 2 or more. 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 .. Each amino acid (aa) shares a common structure; i.e. an amine (NH. 2. ) group, an acid group (COOH), and a central carbon atom bonded to hydrogen and to a side chain (R).. The side chains qualify aas as acidic, basic, neutral, aromatic, and sulphur-containing amino acids.. 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.. 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. Proteins. Part I. Dr. Ravish Chauhan. Associate Professor. IGN College, Ladwa. . . Amino Acids. . These are the compounds which contain both amino and carboxylic group.