PPT-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. 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 . 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.. 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.. 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.. When an amino acid with positive and negative charges is overall neutral in charge, it is said to be at its . isoelectric point (. pI. ). .. . Ball-and-stick model of glycine at its . pI. of 6.0.. 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.. 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. . 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: . Proteins. TextBook. : . HARPERS . REVIEW OF BIOCHEMISTRY. Anatomy of an amino acid. . -Amino acids. A. Example. (glycine). 2-aminoethanic acid. (alanine). 2-aminopropanoic acid. (aspartic acid). 2-aminobutane-1,4-dioic acid. 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..