PPT-Amino Acids

Stryer Short Course Chapter 3 Amino Acid Structure Alpha carbon Sidechain Proteins peptides Stereochemisty Lamino acids Glycine RS vs DL Lisoleucine racemization Ionization 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, . (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.. 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.. THE EXCRETION OF AMMONIUM IONS. A part of NH4+ that is formed in the degradation of amino acids is used for the biosynthesis of nitrogen compounds. In most of the land living vertebrates the excess NH4+ is converted in urea and in that form is excreted. In birds and reptiles it is converted into uric acid and in aquatic animals it is directly excreted as urea.. Debalina. . Mukhopadhyay. . . Containing carbon, hydrogen, nitrogen, oxygen. . Building blocks of protein. . Contain Amino group (NH2+) , carboxyl . group . (COO-) , Alkyl group (R ) / H . . alpha carbon contains the functional groups.. (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.. 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. . Amino Acids. Amino acid play A central role as building block of proteins.. Amino acids also converted to specialized products.. More than 300 different amino acids have been described in nature, only 20 are commonly found in mammalian proteins... . are organic molecules that are the building block of . . proteins. .. -There is 20 . α. -amino acids commonly found in . proteins. . ( . they . have a carboxyl group and an amino group . . . 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 . Presented . by. Ms. . P. . . H. . Giri. Department of Microbiology. Deogiri . College, Aurangabad. B.Sc. F. Y.. Semester II. Paper No. V. Basic Biochemistry. Unit 3 Proteins. Ms. . Priyanka. H. . Giri. 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.. 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.