Information for foreign students


UNIWERSITY OF WARSAW

1 Pasteura Str., 02-093 Warsaw, Poland, phone: +48 (0)22 822 02 11




16


Subject

Principles of Biophysical Chemistry


No / course unit code


Semester

6

Type of course

Lecture


Teaching hours
 per semester    per week

30            2

ECTS credits

2


Lecturer:

Wojciech Dzwolak PhD DSc
Room: 322    Phone extn.: 528    email: wdzwolak@chem.uw.edu.pl

Teaching Division:

Physical Chemistry

Educational and
professional goals:

Introduction to basic concepts of molecular biophysics. Learning how structures and dynamics of proteins, nucleic acids and their biologically-functional assemblies can be accessed experimentally through an array of physical (particularly spectroscopic) methods.

Course description:

Biomolecules: Water and its physical peculiarities in the context of stability and dynamics of biological structures. Conformations of proteins and nucleic acids. Hydrogen bonding in proteins and DNA; ionic pairs; “hydrophobic interactions”.
Biopuzzles: Hierarchies of biostructures. The chirality of life. Methods of structure-determination: diffraction, NMR, circular dichroism, FT-IR. Dynamics of protein conformations: folding, unfolding (denaturation), and aggregation. Conformational transitions in DNA (B-Z). The role of solvent entropy in folding (the hydrophobic core model). The cooperativity of folding: molecular evolution. Molten globule states, chaperones, protein nanopipes, amyloid and prions. Pathways of conformational transitions and folding funnels. Intervention of molecular evolution in polymer science. Conformational disorders: Alzheimer disease and Parkinson diseases. Extremophiles: the spectacular achievements of molecular evolution of proteins. Interactions of proteins and nuclei acids. Viruses as large self-assembling biopuzzles.
Biodevices: Movement and its organization in the nano-scale. Fluorescence and Förster Resonance Energy Transfer (FRET). Elastic complexes of proteins: chaperones, allosteric enzymes, biomotors, myosin-actin, and the molecular basis of muscle contraction. Transmission Electron Microscopy, Atomic Force Microscopy. Molecular Force Microscopy, and Optical Tweezers - or how to stretch a single biomolecule (and what for?). Bio-inspired modern nanomaterials.

Required background:

General Chemistry. Basic knowledge of molecular spectroscopy and biochemistry will be helpful.

Form of assessment:


Written examination (test + problem-solving)

Remarks:

-





Supervisor: Jadwiga Skupinska

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