PPT-Proteins Lecture 5 Introduction

Proteins are polymers of amino acids produced by living cells in all forms of life A large number of proteins exist with diverse functions sizes shapes and structures but each is composed of essential and nonessential amino acids in varying numbers and sequences. 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. . 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 . 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.. Levels of Protein Structure. Primary 1º Structure. The primary structure is simply the sequence of amino acids in a protein.. Chains of amino acids are written from the amino terminus (N-terminus) to the carboxyl terminus (C-terminus).. 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). 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. 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. 4. calories per gram. . The main function of protein is to . build and repair body tissues. .. If carbohydrates and fat are not available, your body will use protein. Is this a good thing? . You must eat protein . 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%). 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. Nutritive function of . proteins.. Quality evaluation.. Proteins: a major food macro-component. . Food is the major source providing proteins to human body:. . food with animal origin. food with . plant. 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.