PDF-Proteins Peptides and Amino AcidsChandra Mohan PhDCalbiochemNova

1 R httpwwwcalbiochemcom Amino Acid and Peptide Nomenclature SystemThe symbol chosen for a given amino acid is derived from its trivial name and is usually the first three letters of this name. Peptide Bond. Amino acid residues in peptides and proteins are linked together through a covalent bond called the peptide bond.. Two amino acid molecules can be covalently joined through a substituted amide linkage, termed a . 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.. 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). Protein . Inference by Generalized Protein Parsimony. Nathan Edwards. Department of Biochemistry and . Molecular & Cellular Biology. Georgetown University Medical Center. Peptide-Spectrum Matches. 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. 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.. 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 . 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).. amino acid. This structure is common to . all . but one of the . α. - amino . acids.. exception . structure, size, and electric charge, and which influence. the . solubility of the amino acids in water. 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. Unit 1 Advanced Higher. Miss Aitken. Pages 16-25. Textbook. Proteomics. Genome:. complete set of DNA. Comprises of coding and non-coding areas. 20-25000 genes in human genome. Proteome:. Entire set of proteins that can be expressed from a genome.