COURSE CONTENT
Introduction
Classification of organic compounds.
-Homologous series, Aromatic character, Stereochemistry, Isomers. Chemical bonds and forces between atoms and molecules.
Factors affecting the rate of chemical reactions. Spectroscopic methods. Concepts of Concentration – Molarity – Solutions.
Acids – bases according to Arrhenius, Bronsted-Lowry, Lewis.
Water dissociation, pH.
Buffers.
Thermodynamics.
Kinetics of chemical reactions.
Amino acids -Structure and properties.
Proteins
-Primary, secondary, tertiary, quaternary structure.
-Forces involved in the formation of protein structures.
-Experimental determination of protein structures.
-Hemoglobin. Structure and function. Effect of 2,3-BPG. Bohr effect. -Allosteric effect, Symmetrical and sequential pattern.
Protein purification and identification -Differential centrifugation.
-Solubility of proteins.
-Chromatography.
-Isoelectric focusing, 2D electrophoresis.
-Antibodies – Immunological methods.
-Mass spectroscopy.
Determination of amino acid sequence.
-Specific cleavage of polypeptides, Separation of polypeptide chains, Synthesis of peptides. -Information we can get from the structure of a protein.
-Protein purification.
Enzymes
-Properties of enzymes.
-Nomenclature of enzymes.
-Thermodynamics of enzymes.
-Active center of enzymes.
– Michaelis-Menten kinetics – KM, Vmax, Kcat/KM -Lineweaver-Burk equation.
-Reactions with many substrates.
-Allosteric enzymes.
-Other factors affecting enzyme activity.
Enzyme inhibition.
-Reversible, Irreversible. Competitive, Non-competitive, Mixed, Non-competitive. Regulation of enzyme activity.
-Compartmentalization.
-Multienzyme systems.
-Proteolytic activation.
Covalent modification.
-Isozymes.
-Allosteric modification.
-Proteolytic regulation.