FSI-TBIAcad. year: 2017/2018
Basic terms of molecular biology. Chemical properties, structure and interactions of nucleic acids and proteins. Methods of biomacromolecules studies, genomics, proteomics, molecular diagnostics. Biosensors, nanotechnology applications in biomacromolecules studies.
Learning outcomes of the course unit
The course facilitates a choice of a diploma project by a student and provides him/her basic knowledge on molecular biology as well as interdisciplinary themes at frontiers of molecular biology, physical and analytical chemistry, biophysics, nanosciences and biomedical applications.
Basics of physics, inorganic, organic and physical chemistry, biochemistry and general biology
Recommended optional programme components
Recommended or required reading
ROSYPAL S. Úvod do molekulární biologie
LODISH H. et al.: Molecular Cell Biology (Freeman and Co., 2003)
BLACKBURN GM and GAIT MJ.: Nucleic Acids in Chemistry and Biology (Oxford University Press 1996 - second edition)
NEČAS, O. a kol.: Obecná biologie, H & H, Praha, 2000.
ALBERTS, B. a kol: Základy buněčné biologie. Espero Publishing, Ústí nad Labem, 2001.
WATSON J.D.a kol: Rekombinantní DNA, Academia Praha, 1988
PALEČEK, E et al. (ed.): Electrochemistry of nucleic acids and proteins. Towards electrochemical sensors for genomics and proteomics, Elsevier 2005
Planned learning activities and teaching methods
The course is taught through lectures explaining the basic principles and theory of the discipline. Exercises are focused on practical topics presented in lectures. Teaching is suplemented by practical laboratory work.
Assesment methods and criteria linked to learning outcomes
The assessment of a student is made upon his performance in practice and quality of a discussion on topics selected at the examination (lecture notes allowed at preparation).
Language of instruction
Educate the students in basics or molecular biology, particularly in properties of nucleic acids and proteins. The emphases will be put to physico-chemical properties of biopolymers and utilization of these properties in bioanalytical applications, biosensors and nanotechnologies.
Specification of controlled education, way of implementation and compensation for absences
The presence of students at practice is obligatory and is monitored by a tutor. The way how to compensate missed practice lessons will be decided by a tutor depending on the range and content of the missed lessons.
Type of course unit
39 hours, optionally
Teacher / Lecturer
Definition of the molecular biology subject. From atoms and molecules to living cells. Nucleic acids, proteins, lipids, polysaccharides. Chemical nature of biomacromolecules, basic interaction types. Organized structures, membranes, organelles, prokaryotic and eukaryotic cells. (0-6 lessons)
Structure and interactions of nucleic acids. DNA double helix. Left-handed DNA, hairpins, triplexes, tetraplexes. DNA supercoiling. Replication, transcription, recombination. Chemical reactivity of nucleic acids, non-covalent interactions. DNA damage and repair, mutagenesis. Nucleic acids-processing enzymes. RNAs and their biological functions. (7-20 lessons)
Methods of the nucleic acids studies. Optical methods, electrophoresis, Southern and northern blotting, DNA sequencing, DNA hybridization, PCR, enzymatic and chemical probes of DNA structure, DNA footprinting. Recombinant DNA. Synthetic analogues of nucleic acids, DNA labeling. Biosensors, gene chips, genomics. Electrochemistry of nucleic acids, interactions with electrically charged surfaces. Aptamers. Nanotechnology in nucleic acids analysis. (21-28 lessons)
Proteins. Amino acids, primary, secondary, tertiary and quaternary structure of proteins. Conjugated proteins. Genetic code and proteosynthesis. Denaturation and aggregation of proteins. Protein engineering. Nucleic acids-protein interactions. (29-34 lessons)
Methods of protein studies. Optical methods, electrophoresis, western blotting, immunochemical techniques. Chemical probes, protein sequencing. Proteomics, 2D electrophoresis, mass spectrometry. Protein chips, immunosensors, enzyme sensors. Protein electrochemistry; conjugated proteins bearing reversible redox centers and non-conjugated proteins, catalytic hydrogen evolution on mercury and amalgam electrodes. Nanotechnology in protein analysis. (35-39 lessons)
20 hours, compulsory
Teacher / Lecturer
Discussion of lectured themes, practicing, solving worked examples.
labs and studios
6 hours, compulsory
Teacher / Lecturer
Practical demonstrations of methods of the nucleic acids and protein analysis in laboratories of the Institute of Biophysics, ASCR, v.v.i.