PPT-Amino Acids, Peptides, Proteins and Nucleic Acids

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 Streckers synthesis. 2. Proteins. Proteins are polymers made of monomers called amino acids. All proteins are made of 20 different amino acids linked in different orders. Proteins are used to build cells, act as hormones & enzymes, and do much of the work in a cell. 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). polymers. four major classes of biologically important organic molecules: . carbohydrates. lipids. proteins . (and related compounds). nucleic acids . (and related compounds). Discuss hydrolysis and condensation, and the connection between them.. Unit objectives:. Identify amino acid classifications based on nutritional use and chemical properties of side chains. Describe the primary, secondary, tertiary and quaternary structures of 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 . . . 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. . A. PHYSICAL PROPERTIES. Optical properties: . All amino acids except glycine possess optical isomers due to the presence of asymmentric carbon atom. Some amino acids have a second assymmentric carbon e.g. isoleucine, threonine.. 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 . Amino Acids are the building units of proteins.. The main role of amino acids is in the synthesis of structural and functional . proteins.. The . non-essential amino acids are either derived from the. A. . Peptides. are compounds, formed of less . than . 50 . amino acids . linked together by peptide bonds.. 1.. . Dipeptide. (2 amino acids and one peptide bond).. 2.. . Tripeptide. (3 amino acids and two peptide bonds).. Metabolism is the sum of all biological processes. . There are 2 major metabolic processes. Anabolism – the building up of complex molecules. Catabolism – the breaking down of complex molecules. Macromolecules. Proteins. Part I. Dr. Ravish Chauhan. Associate Professor. IGN College, Ladwa. . . Amino Acids. . These are the compounds which contain both amino and carboxylic group.