PPT-Amino Acids, Polypeptides and

Proteins TextBook HARPERS REVIEW OF BIOCHEMISTRY Anatomy of an amino acid Amino acids A Example glycine 2aminoethanic acid alanine 2aminopropanoic acid aspartic acid 2aminobutane14dioic acid. (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.. 2. : Molecular Biology. 2.4 Proteins. Learning objectives. U: amino acids are linked together by condensation to form polypeptides. U: There . are 20 different amino acids in polypeptides synthesized on ribosomes.. 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, . 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. 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.. (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.. 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 .. 6. 6.1 Differentiate . between essential amino acids and nonessential amino acids.. 6.2 List . the functions of protein in the body.. 6.3 List . the steps for protein digestion and absorption in the body. . 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.. 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 . Protein. Builds and repairs body tissue. Provides some energy. There are 4 calories per gram of protein. Protein. Composed of chains of amino acids. Common Amino Acids. Alanine. Glycine. Isoleucine. Leucine. 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. Proteins. Part I. Dr. Ravish Chauhan. Associate Professor. IGN College, Ladwa. . . Amino Acids. . These are the compounds which contain both amino and carboxylic group.