PPT-Expanding the Genetic Code with Unnatural Amino Acids

Kevin Cravedi Biochemistry BS Class of 2010 Department of Chemistry Senior Seminar March 11 2010 Thesis Background of Method Application of Method Example 1 AzoPhe Example 2 Sulfotyrosine Sulfohirudin. 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 . 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.. B.2. Properties of 2-amino acids . (B.2.2). Zwitterion. (dipolar) . amino acids contain both acidic and basic groups in the same molecule . therefore, are . amphoteric. in nature (capable of behaving as acids or bases). Plants and bacteria produce all of their amino acids using NH. 4. +. and NO. 3. –. .. Humans can synthesize 9 of the 20 amino acids found in their proteins.. Nonessential amino acids are synthesized in the body, while essential amino acids must be obtained from diet.. (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). 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: . ). Dr. . Sumbul. . Fatma. Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. Non-standard amino acids.. . 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 . S P T SCIENCE COLLEGE. (SHRI GOVIND GURU UNIVERSITY). Genetic code is the term . used . for the way . . the four bases of DNA--the A, C, G, and Ts--are . strung/arranged . together in a way that the cellular machinery, the ribosome, can read them and turn them into a protein. 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 “.