PPT-Analysis of Proteins

Lecture 7 1 Protein Characterization 2 Absorbance Spectroscopy The aromatic amino acids all have characteristic absorbance profiles 5500 M 1 cm 1 1490 M 1 cm 1 Also Cysteine. . from lack of structure to. pleiotropy. of functions. Lilia Iakoucheva. University of California, San Diego. Ordered Proteins. Disordered Proteins. Uversky and Dunker, 2012, Anal . Chem. Outline. 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. . 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 . PROTEINS – (DR. TRAISH) Introduction to Proteins - Proteins are abundant and functionally diverse molecules - They participate in cell regulation at all levels - They share a common structural 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.. 2. Proteins (. Polypeptides. ). Chains of Amino acids (. 20. different kinds). bonded together by . peptide bonds. . (. polypeptides. ). Made of . Nitrogen, Carbon, Oxygen, and Hydrogen. Functions:. 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). Different types of . mb. proteins require different conditions for . mb. release. Integral membrane proteins directionally insert in the membrane bilayer. Outside cell. Inside cell. Glycophorin. and . 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. In order to survive, the human body needs the nutrients found in food. These nutrients, which perform a number of life-sustaining functions in the body, are divided into 6 main categories: carbohydrates, proteins, fats, vitamins, minerals and water. Each has a unique function in the normal growth and repair of the body.. Jenny Zhou and Anne Ye. 12-9-11. Fan, . Vermesh. , . et al. . Nature Biotechnology (2008).. Motivation and Design Considerations. Blood is the most important fluid for clinical diagnostics. Current clinical assays only analyze a handful of plasma proteins. 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.. 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 .