PPT-Polypeptides and proteins -3

Lecture 1 With DrHamzeh Al Share MD Original Slides for Prof Sameeh Al Saraireh Final 1 1 Fibrous proteins  These proteins have a rod like structure They are not. Dina N Kovarik, MS, PhD. Digital World Biology. Updated . April 24, 2015. Fluorescent Proteins are Valuable Tools. Locate proteins in the cell. Track the migration of cells. Reporter of expression. Sister centromeres . 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.. α-helical polypeptides . Polypeptides are . biomedically. important polymers due to their minimal cytotoxicity, proteolytic degradability and the capability to adopt secondary structures reminiscent of naturally occurring . 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). 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 . Most abundant molecule in cells making up 50% or more of their dry weight. Every protein has a unique structure, or shape. Allows it to perform a specific function. Enzymes are proteins that function as catalysts for many reactions in foods. Dna. , Proteins and Binding to ligands. Think. What proteins are associated with DNA? . How are proteins involved in transcription?. How is protein production controlled?. Why is it important that protein production is controlled?. 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.. Biocompatibility and Cellular Overview Part 2. Outline . Biocompatibility. Quick overview of cellular interaction. Scale, size, generic animal cell. Nanoscale materials . for biological interaction. Liposomes. The concentration of many of these are affected by pathological processes; they are therefore measured.. They contain disulphide bonds.. Functions of plasma proteins include:. Transport. Maintaining plasma . Size. Colloidal solutions. Charge. UV absorption. Solubility. Physical properties. Molecular weight. :. Vary from. 6000 . to million Daltons (Da) . Protomeric. proteins. : 50. . 000 . to. 100. . 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.