PPT-PROTEINS Proteins are polymers of amino acids referred to as polypeptides.

Each amino acid aa shares a common structure ie 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 sulphurcontaining 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.. Formations and linkages. What are polymers?. Alkene. molecules have the ability to add onto one another and produce large molecules these are polymers. . Therefore what are monomers?. The process of these large molecules forming is termed addition polymerisation.. The 411. Proteins account for more than 50% of the dry mass of most cells. Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances. 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.. 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, . 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.. Carbohydrates, lipids, proteins, and nucleic acids. Monomers. Glucose. Amino acids. Nucleotides . Fatty acids . Polymers. Carbohydrates . Nucleic acids. Lipids . Proteins . Carbohydrates. The word carbohydrate literally means “watered carbon.”. 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.. 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. . 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 . Biocompatibility and Cellular Overview Part 2. Outline . Biocompatibility. Quick overview of cellular interaction. Scale, size, generic animal cell. Nanoscale materials . for biological interaction. Liposomes. 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. 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. Acids. By . Professor . Dr. Jamal Ahmed Abdel -Barry. . Rare Amino Acids. In addition to 20 standard amino acids there are several amino acids that can be isolated from the hydrolysis of special type of protein, all are derivatives of some standard amino acids..