PPT-1 Proteins

Author : olivia-moreira | Published Date : 2017-05-30

2 Proteins Polypeptides Chains of Amino acids 20 different kinds bonded together by peptide bonds polypeptides Made of Nitrogen Carbon Oxygen and Hydrogen

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1 Proteins: Transcript


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. Suarez, R. Martinez, O. Diaz, H. Jones, T. Ashraf, E. Priddis, K. Durham, Undergraduate Biology Research, Cochise Community College, Sierra Vista, AZ . INTRODUCTION.  . Genomic and proteomic studies can reveal multi-dimensional aspects of biological model organisms. DNA sequencing and short tandem repeats are utilized to characterize organism’s phylogenetic relationships; another approach is to study their various proteins. Many genomic studies utilize extraction and amplification of nucleic acids to help make detection more straightforward. There is no proteomic procedure similar to PCR that would identify proteins at their naturally existing concentration, as well as the presence of many other proteins for comparative studies. Most methods for studying proteins revolve around running 1D, 2D, or 3D gels, and comparing and identifying similar proteins. . 2. Proteins. Proteins are polymers made of monomers called amino acids. All proteins are made of 20 different amino acids linked in different orders. Proteins are used to build cells, act as hormones & enzymes, and do much of the work in a cell. Protein. The . main function of protein is to . build and repair tissues . (muscle tissue). Protein. Protein can be a source of energy but should be used as a last resort. Effect of pH and . Ionic Strength . on Solubility of Proteins. INTRODUCTION. Food Industry:. - Functional Properties - Nutritional. Gelation. Foaming. Change in viscosity. Examples. : . Whole eggs, egg yolk, egg albumen, whey solids, non-fat dry milk . . from lack of structure to. pleiotropy. of functions. Lilia Iakoucheva. University of California, San Diego. OUTLINE. Characterization . and properties of IDPs. . Functional repertoire of IDPs. 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). 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. 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.. Learning Targets. :. * Understand . denaturation . of protein . . * Tell . some of its causes and effects. Complete. protein comes from . animal. products. Incomplete. protein comes from the . SEEDS. proteins of milk, meat and eggs.. Milk composition. Deficient in iron and vitamin C. Milk proteins. Total protein content in milk – 2.9 – 3.5%. Two major types of milk protein. Caseins (80%). Whey proteins: (20%). Chromatin is made of repeating units of nucleosomes, which consist of 146 base pairs of DNA wrapped around an octamer of four core . histone proteins (H3, H4, H2A and H2B). Introduction. Histones are a special group of proteins found in the nuclei of eukaryotic cells responsible for DNA folding and chromatin formation.. 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 .

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