Code: 
BIOL-256
Semester: 
D Semester
Course Type: 
Obligatory
Course units:
4
ECTS units
6
Hours per week
Theory: 4

Description

Objectives of the course (preferably expressed in terms of learning outcomes and competences): The main goal of the course is to offer a global understanding of physical chemistry through studying the basic principles. The exploitation of physical chemistry in biology is manifested by biological examples.

Course contents:

Physical chemistry is organized in two major fields in respect to the macroscopic or microscopic nature of the subjects studied. The macroscopic field covers the following groups of subjects:

Introduction: Units, the ideal gas laws, real gases, van der Waals and Virial equations, condensation of gases, the critical state, the kinetic theory of gases, the relationship of kinetic energy to temperature and equipartition.
Thermodynamics: The laws of thermodynamics, enthalpy, entropy, Gibbs and Helmholtz energies, thermochemistry, the Carnot heat engine, heat pumps, refrigerators, air-conditions and phase diagrams.
Nonelectrolyte and electrolyte solutions: Mole fraction, Molarity, molality, partial molar volume and Gibbs energy, colligative properties, degree of electrolyte dissociation, ionic activity, Debye-Huckel theory, salting-in, santing-out, the Donnan effect, osmosis, biological membranes and membrane transport.
Chemical equilibrium: Reactions in solution, binding of ligands and metals to macromolecules, bioenergetics, the standard state in biochemistry, ATP-the currency of energy, principle of coupled reactions and glycolysis.
Electrocemistry, Acids and bases: Electrochemical cells, Nernst equation, determination of pH and activity coefficiencents, biological oxidation, membrane potential, acids and bases dissociation, salt hydrolysis, buffer solutions, isoelectric point and blood pH.
Chemical kinetics and enzyme kinetics: Reaction rate, order and molecularity, complex reactions, Arrenius equation, collision theory, transition state theory, general principles of catalysis, Michaelis-Menten and steady-state equations, multisubstrate systems, enzyme inhibition and allosteric interactions.

The microscopic field covers the following groups of subjects:

Quantum Mechanics: Wave theory of light, Planck's quantum theory, Heisenberg’s uncertainty principle, Schrodinger’s wave equation, quantum-mechanical tunneling, atomic orbitals and the periodic table.
The Chemical Bond and intermolecular forces: Valence bond theory, molecular orbital theory, resonance and electron delocalization, the peptide bond, coordination compounds, ionic bond, London interactions, repulsive and total Interactions, sickle-cell anemia, hydrogen bond, structure and properties of water, and hydrophobic interaction.
Spectroscopy: Beer-Lambert law, microwave, infrared, electronic, nuclear magnetic resonance (NMR), electron spin resonance (ESR) spectroscopy, fluorescence (Liquid Scintillation Counting), phosphorescence, lasers and Fourier- Transform spectroscopy.
Molecular Symmetry, Optical Activity, Solid and Liquid State: Symmetry of molecules, optical activity, polarized light, circular dichroism, crystal systems, structure determination by X-ray and neutron diffraction, viscosity and surface tension.
Photochemistry and Photobiology: Thermal versus photochemical reactions, the atmosphere, the greenhouse effect, photochemical Smog, polar ozone holes, photosynthesis, photosystems I and II, vision, biological effects of radiation and light-activated drugs.
Macromolecules: Size, shape, and molar mass determination of macromolecules, ultracentrifuge, viscosity, electrophoresis, configuration and conformation, random-walk model, structure of proteins and DNA, denaturation and protein folding.