1. Structure and function of proteins Amino acids as the basic components of proteins Primary structure of proteins: amino acid sequence Secondary structure of proteins: alfa helix, beta-sheets, loop, turn Tertiary structure of proteins: soluble vs. insoluble (membrane) proteins Quarternary structure of proteins: multisubunit complexes of proteins Amino acid sequence of proteins determines their 3D structure 2. Principal biochemical methods to study proteins Purification of proteins: salting out, dialysis, chromatography, 1D and 2D electrophoresis, ultracentrifugation, immunochemical methods (Western blotting, ELISA, immunofluorescence) Determination of the amino acid sequence by N-terminal Edman degradation, mass spectrometry Peptide synthesis Determination of 3D structure of proteins: NMR, X-ray analysis 3. Nucleic acids (DNA, RNA) and the flow of genetic information Composition of DNA and RNA: sugars, type of bases, formation of the chain Structura of DNA and RNA: double-helix, complemetarity of bases, replication DNA polymerases: the enzyme catalyzing formation of a new complementary chain Gene expression: transformation of the genetic information into the functional molecule (transcription, translation) Mozaic structure of eukaryotic genes: exons and introns, splicing 4. Basic tools for the study and manipulation of genes and their expression (Tichý) Methods of recombinant DNA: restriction and ligation, preparation of plasmids and vectors for introducing DNA inside rthe cells, their expression, synthesis of oligonucleotides, PCR Manipulation of genes: exploring their expression, introducing new genes into organisms (transgenosis), removal of genes and preparation of their site-directed mutations Genomics and proteomics 5. Enzymes (Masojídek) Basic characteristics Termodynamcs of enzyme catalysis Basic kinetics of the enzyme catalysis: model of Michaelis-Menten Coenzymes and vitamins Enzyme inhibition: competitive, non-competitive, irreversible Strategy of catalysis: examples Regulation of enzyme catalysis: allosteric inhibition, isoenzymes, proenzymes 6. Sugars Monosaccharides as aldehydes or ketons with several hydroxyl groups Oligosaccharides and polysaccharides Binding of sugars to other macromolecules, lectins 7. Lipids and membranes Fatty acids Three basis types of membrane lipids: phospholipids, glycolipids and cholesterols Interaction lipid-protein: membrane proteins Transport of substances across the membrane, membrane channels and pumps 8. Principles of cellular metabolism Macroergic bonds, ATP as the universal source of energy for biosynthetic reactions Regulation of metabolism via regulation of the amount and catalytic activity of enzymes, and via regulation of accessibility to substrates Regulation of metabolism from outside (signal transduction pathways) 9. Glycolysis, glukoneogenesis, metabolism of glycogen, lipids and fatty acids Degradation of sugars as an important source of energy: glycolysis Glukoneogenesis Metabolism of glycogen Metabolism of lipids and fatty acids 10. Metabolism of proteins, amino acids and nucleotides Proteins, their turnover Principles of amino acid degradation: removal of ammonia and carbon skeleton Principles of nucleotide degradation 11. Cycle of tricarboxylic acid, respiration and oxidative phosphorylation Cycle of tricarboxylic acid Respiration Oxidative phosphosforylation 12. Photosynthesis Light reactions of photosynthesis Dark (Calvin cycle) a pentose cycle
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Jeremy M. Berg, J.L. Tymoczko, L. Stryer. Biochemistry, The 5th edition. W.H. Freeman and Company New York, 2002. ISBN 0-7167-4684-0.
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Komenda J., Masojídek J., Tichý M. powerpointová presentace. ÚFB Nové Hrady, 2003.
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VODRÁŽKA Z.:. Biochemie. Academia Praha, 1996. ISBN 80-200-0600-1.
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