Βiochemistry - Βiotechnology

The course aims at teaching all subjects and laboratory methods of biochemistry and Principles of Biotechnology necessary to Agricultural Technology, both in future courses (eg Physiology (plants or animals), Soil Science, Pharmacology, Plant nutrition, Lubrication plants, Animal Nutrition) but also in daily practice after the graduation.

Objectives

Learning objectives Chapter 1) Learn how various molecules shown. Advantages disadvantages of each method. Understand the importance of electrostatic interactions, hydrogen bonding forces and van der Waals. Learn why the polarity and the consistency of water is important for its biological role. Importance of water as a solvent. Meaning of hydrophobic interactions.   Chapter (2) Structure and function of amino acids Peptide group. Features (rigid and flat). The proteins were determined by amino acid sequence (primary structure). Protein trunk given a specific shape in space (secondary structure). A polypeptide chain having a single three-dimensional form (tertiary structure). Some proteins are composed of two or more polypeptide chains of a given embodiment of each relative to the other (tertiary structure). The sequence of amino acids determines the three dimensional structure (Anfinsen experiment). The essence of the action of proteins: specific commitments and transmission configuration changes.   Chapter (3) Methods for separation and purification of proteins.   Chapter (4) Know that enzymes are biological catalysts that accelerate each reaction catalyzing thousands to millions of times, that have a high degree of specialization, and that their catalytic activity is regulated. Understand the terms of coenzyme, substrate, cofactor. Be aware that the enzymatic reactions reach a maximum speed, as long as there is excess ypostomatos. Be aware that there are inhibitors of the action of each enzyme. The two main classes of inhibitors are competitive and non-competitive. You can give a physico-chemical explanation of the type of modification of the enzyme activity that brings each.   Chapter (5) Understand that vitamins are divided into fat-soluble group (A, D, E) and water-soluble (B, C) group. Be aware that all vitamins are the same or derivatives cofactors of enzymes or key modulators of cellular receptors (eg Vit. A, D), and substances which most organizations can not synthesize, but require ready, Hence the name. Understand the role of ATP in biochemical reactions. To get a sense of the general visa metabolism (glycolysis, citric acid cycle, oxidative phosphorylation, urea cycle) Chapter 6) Understand the properties and function of the enzyme acid HIV protease (suspension etc.) To understand the difference in the operation of a single enzyme (eg carboxypeptidase) by an allosteric enzyme (aspartic transcarbamoylase). What is the role of allosteric modulators and what biological significance. Chapter (7) Understand what is limiting enzyme. Understand the terms, cohesive ends, plasmid, phage. Understand in which way you use restriction enzymes and plasmids, we can insert foreign DNA into a host cell. Understand how to mass produce foreign proteins in host cells (of various kinds). Realize that these processes may be made in plant cells and ponder their meaning. Chapter (8) Understand the chemical structure of carbohydrates. Behold how we come to common aldoses glucose and galactose from glyceraldehyde. Understand the open and closed chain structures, forms tub and daybed. Understand that sugars may contain amines, increasing their complexity. Know the importance of O- and N-glycosidic bond to the formation of complex compounds with the sugars. Know the main types of saccharide polymers (cellulose, glycogen, amylose, amylopectin, chitin) and chemical basis for differences in physical characteristics. Chapter (9) To understand the structure of lipids, and thus the fluid mosaic of biological membranes (cellular and these organelles) and the many advantages that this structure gives the various cells. Chapter (10) Understand experiments with which Avery and his colleagues concluded that DNA is the genetic material. Understand that DNA is a double stranded antiparallel and the specific base pairing can always know the second strand sequence, as long as we know the sequence of the first strand. Understand how the replication of DNA, what enzymes need and what properties they have. Chapter (11) Know the types of RNA present in the cell and the function of each one. Be aware that the RNA is complementary structure of DNA, based on the mating status of the bases. Know the properties of the enzyme RNA polymerase. Chapter (12) Know the properties of the genetic code (colinear, without punctuation, degenerate) and what each of them means. Know how are carrying out protein synthesis in cells: what organelles and what enzymes and other molecules needed. Chapter (13) To know the mechanisms of gene regulation

Prerequisites

The course of Agricultural Chemistry, 1st semester.

Syllabus

The detailed description of the course is as follows: A. Lecture (2 hours per week) 1. Introduction, organic molecules, double bonds, properties of water, buffers 2. Amino acids, proteins and protein structure function 3. Exploration of proteins 4. Enzymes, coenzymes, cofactors, kinetic 5. Vitamins 6. enzymes, inhibitors, action mechanisms 7. Enzymes, mechanisms of action, setting action 8. sugars, monosaccharides polysaccharides 9. Lipids, cell membranes 10. Structure and function of DNA 11. Structure and function of RNA, restriction enzymes, recombinant DNA, polymerase chain reaction, biotechnology applications (synthetic vaccines, proteins, transgenic plants) 12. Synthesis of proteins and genetic code 13. Regulation of genes in prokaryotic and eukaryotic organizations In the documents, some will find a detailed description of the program of lectures, literature etc. of the course. Also, there will be posted all the useful sites that help in further understanding of the subject of Biochemistry.