LECTURES

The lectures will take place on Mondays at 12:45 in the lecture hall of Collegium Universum, Mickiewicza 2c.

The first lecture will be on September 5th.

SEMINARS

They are online on Blackboard platform.

CLASSES

They take place in student laboratories of the Department of Medical Biochemistry (Collegium Universum, 3^rd floor).

The laboratory classes will start on Monday, October 5th at 8:15 am and 2:45 pm (according to dean groups).

Please, take with you lab coat, soft footwear and Biochemistry Workbook (can be borrowed in the library or print first class from Biochemistry workbook .pdf version in Recomended handbooks on website of Department of Medical Biochemistry).

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       tuesday 12:30 - 13:30
Tomasz Gogiel       friday     9:00 - 10:00
Lech Romanowicz  friday     9:00 - 10:00
Anna Tokarzewicz  friday     9:00 - 10:00

Katarzyna Miniewska  thursday 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),

Inborn defects in protein structure – hemoglobin, collagen

collagen triple helix;

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