Bi7230c Advanced methods of biophysics in experimental biology - practice

Faculty of Science
Autumn 2008
Extent and Intensity
0/2/0. 2 credit(s) (plus extra credits for completion). Recommended Type of Completion: k (colloquium). Other types of completion: z (credit).
doc. Mgr. Ctirad Hofr, Ph.D. (seminar tutor)
doc. RNDr. Jan Hejátko, Ph.D. (seminar tutor)
Mgr. Michal Zimmermann, Ph.D. (seminar tutor)
RNDr. Terezie Mandáková, Ph.D. (seminar tutor)
Mgr. Pavla Šilerová (seminar tutor)
Guaranteed by
prof. RNDr. Jiří Fajkus, CSc.
Department of Experimental Biology - Biology Section - Faculty of Science
Contact Person: doc. Mgr. Ctirad Hofr, Ph.D.
Prerequisites (in Czech)
NOW ( Bi7230 Adv. Methods of Biophysics )
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
The capacity limit for the course is 30 student(s).
Current registration and enrolment status: enrolled: 0/30, only registered: 0/30, only registered with preference (fields directly associated with the programme): 0/30
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Course objectives
The main objective of the practical training course is to acquire practical experience with modern spectroscopic methods employed in the analysis of protein-protein and protein-DNA interactions. From the methodical approaches, the main emphasis is put on highly sensitive fluorescent methods and their practical use in biological laboratories. The practical one week course, complementing lectures of Bi7230, enables trainees to corroborate their theoretical knowledge about methodical principles using modern instrumentation of research laboratories. Training is focused on the effective development of skills required for application of specialized techniques. These techniques have become indispensable for recent tasks of basic and applied research in today’s interdisciplinary concept of biological sciences.
  • Spectral characterization of proteins and nucleic acids
  • Accurate determination of concentration of nucleic acids and proteins by fluorescence and absorption spectroscopy (colorimetry)
  • Effects of pH and temperature on spectral properties of fluorophores
  • Measurement of intrinsic fluorescence of BSA, tryptophan, and thyroxin
  • Preparation of fluorescently labeled DNA
  • Spectroscopic characterization of fluorescently labeled DNA
  • Visualization of macromolecules after electrophoretic separation
  • Use of resonance energy transfer (FRET) for detection of DNA hybridization
  • Fluorescence quenching after relaxation of loop structure of fluorescently labeled DNA
  • Real-time PCR – Detection of DNA amplification
  • Fluorescence microscopy (fluorescence in situ hybridization)
  • Fluorescence anisotropy – Study of protein binding to a fluorescently labeled DNA
  • Lakowicz J.R.: Principles of Fluorescence Spectroscopy. Third Edition, Springer + Business Media, New York, 2006
Assessment methods
Language of instruction
Further Comments
The course is taught annually.
The course is taught: in blocks.
Teacher's information
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2007, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012.
  • Enrolment Statistics (Autumn 2008, recent)
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