PPT-Proteins:Amino

acids Need to book Molymods CHO amp N each group needs 16 single bonds 4 double bonds 4 Carbon 2 Nitrogen 4 oxygen 10 hydrogen Practical activity 21 ALSO Need to give Mel 2 weeks notice on the chromatography . The 20 different amino acids. 7.5.1: Explain the four levels of protein structure, indicating the significance of each level.. Peptide bonds link the amino acids together . Polypeptide with five amino acids. . The 20 different amino acids. 7.5.1: Explain the four levels of protein structure, indicating the significance of each level.. Peptide bonds link the amino acids together . Polypeptide with five amino acids. . Importance, Characteristics, Structure, Classification, . Denaturation. Importance. Major structural components of animal tissues. Involved in the maintenance of life processes as communication (nerves), defense (antibodies), metabolic regulation (hormones), biochemical catalysis (enzymes), and oxygen transport (hemoglobin). 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.. 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. Amino . Acids. In a transamination reaction, . aspartate transaminase (AST) . catalyzes the reversible transfer of an amino group between glutamate and aspartate.. an . α. -amino group is transferred from an amino acid to an . 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. . for . life.. . The importance of proteins was recognized by chemists in the early 19th century, including Swedish chemist . Jöns. Jacob Berzelius. , who in 1838 coined the term . protein. , a word derived from the Greek . 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. Dissociation. Optical Activity. Solubility, Hydration and Swelling Power. Dissociation. Proteins, like amino acids, are amphoteric.. Depending on pH, they can exist as polyvalent (cations, anions or . Color Tests for Proteins and Amino Acids. B)Color Test for Specific Amino Acids. 1/. Millon's. Test:. *Used for detecting the presence of . monohydroxybenzene. derivatives (. e.g. : Tyrosine, Tyrosine derivatives, Phenol).. 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. Explain the formation . of a protein.. Classify proteins according to their chemical structure.. Describe the classification of protein.. Name a food source for the following proteins: albumin . caseinogen. Lecture by. :. . Dr. . Samia. . Naz. . (APWMO). Biochemistry Department, KEMU. Introduction. Proteins are the primary constituents of body. .  . These are genetically designed sequences of amino acids linked together by peptide bonds. .