The biochemistry lectures will be on 7th of October 2024, in Collegium Universum lecture hall.
SEMINARS
Subjects indicated for self-development;
They are online on the Blackboard platform.
coordinator: dr hab. Lech Romanowicz
e-mail: lech.romanowicz@umb.edu.pl
phone: +48 (85) 748 55 78
consultations:
Justyna Bączyk thursday 9:00 - 10:00
Marta Bruczko-Goralewska friday 9:00 - 10:00
Tomasz Gogiel friday 9:00 - 10:00
Lech Romanowicz friday 9:00 - 10:00
Anna Tokarzewicz friday 9:00 - 10:00
Credit I
Proteins
Structure of amino acids
Classification of amino acids (polarity, charge):
non-polar: Gly, Ala, Val, Leu, Ile, Phe, Trp, Met, Pro
polar without charge: Ser, Thr, Tyr, Asn, Cys, Gln
acidic chains: Asp, Glu
basic chains: His, Lys, Arg
Peptide bond
Nomenclature of peptides
Biological importance of peptides (with examples)
Protein structure: I, II (alfa-helix, beta- sheet), III (myoglobin), IV (hemoglobin), collagen triple helix;
Inborn defects in protein structure - hemoglobin
Denaturation of proteins
Properties of proteins in solution (solubility, amphoteric properties, pI)
Isolation of proteins from biological materials: Column chromatography - size exclusion chr., ion exchange chr., affinity chr., HPLC; PAGE, isoelectric focusing, the Edman reaction
Protein functions
Enzymology
Definition of metabolism, anabolism, catabolism
Equilibrium of chemical reaction
Activation energy, free energy
Mechanism of the enzymatic reaction
Enzyme active site
Enzymatic reaction velocity and its dependence on: temperature, pH, substrate concentration, allosteric effectors (positive and negative)
Maximal velocity (Vmax) and Michaelis constant (Km)
Enzyme activity - units
Inhibitors
Proenzymes and their conversion to active forms
Regulation of enzyme activity
Multifunctional enzymes on the example of: phosphofructokinase-2,
fructose 2,6-bisphosphatase, fatty acid synthase
Multienzyme complexes on the example of:
pyruvate dehydrogenase, α-ketoglutarate dehydrogenase
Enzyme specificity
Coenzymes
Isoenzymes on the example of: lactate dehydrogenase,
creatine kinase, malate dehydrogenase, glycerol-3-phosphate dehydrogenase,
hexokinase
Classification of enzymes, international enzyme code
Application of enzymes in medicine and biotechnology:
markers of disease – aminotransferases
drugs – asparaginase
reagents – urease
gene therapy
Bioenergetics
Exergonic reactions and endergonic reactions
ATP as an energy relay
High-energy compounds
Low-energy compounds
Oxidative phosphorylation
Substrate phosphorylation
Mitochondrial respiratory chain
Respiratory complexes
Transport of protons and electrons through respiratory chain
Chemiosmotic theory
Blocking the respiratory chain
Uncoupling of oxidative phosphorylation
Reactive oxygen species
Carbohydrate metabolism
Trioses, tetroses, pentoses, hexoses
Glucose, mannose, galactose, fructose
Straight-chain form, cycle form, alpha and beta form
Aerobic and anaerobic glycolysis (with structures)
Regulation of glycolysis
Energy balance of glycolysis
Oxidative decarboxylation of pyruvate
Krebs cycle (with structures)
Credit II
Gluconeogenesis (with structures)
Pentose phosphate pathway – course, biological importance
and connection to glycolysis and gluconeogenesis
Fructose metabolism and hereditary defects: essential fructosuria, hereditary fructose intolerance
Galactose metabolism and galactosemias
Derivatives of simple sugars: glycosides, uronic acids, aminohexoses, sialic acid
Disaccharides: maltose, isomaltose, sucrose (saccharose), lactose
Polysaccharides: starch, glycogen
Biosynthesis and degradation of glycogen
Regulation of glycogen metabolism
Inborn defects in glycogen metabolism