INTERNATIONAL BURCH UNIVERSITY
Graduate Study - Faculty of Engineering and Natural Sciences
3+2 Genetics and Bioengineering
||Purification Techniques of Biomolecules
||Number of ECTS Credits
||Class Hours Per Week
||Total Hours Per Semester
|The course gives an orientation in the methods that are used for purifying biomolecules. Focus will be on proteins, but other biomolecules will also be treated.The course describes: Methods to prepare cell extracts and preparation of samples. Centrifugation, filtering. Precipitation. The theoretical and practical bases of chromatography. Gel-filtration, ion exchange chromatography, hydrophobic interaction chromatography, reverse-phase chromatography, affinity chromatography, etc.
|Purification Techniques of Biomolecules course is designed mainly to accomplish the following objectives;
Explain the intermolecular interactions: mechanism of covalent and noncovalent interactions, charge-charge interactions, hydrogen bonds, Van der Waals forces and hydrophobic interactions.
Describe ionization of water: acid/base chemistry as it applies to biological molecules.
Comprehend structure and function: basic molecular properties of the 4 classes of biological molecules (proteins, carbohydrates, lipids and nucleic acids) and the subunits from which they are formed. Explain how the structure of biological molecules dictates function and how changes in structure direct biochemical reactions.
Define organic reaction mechanisms: the network of chemical reactions that make up central metabolism.
Acquire general background in the field of purification of biomolecules: comprehend scientific literature pertaining to subject matter in purification stratagies.
Approach to scientific mysteries: apply knowledge & concepts to novel problems
- Introduction; the chemical elements of life, introduction to biomolecules
- Matter, elements, atoms, subatomic particles, intermolecular interactions; covalent-iyonik-hydrogen bonds, van der waals interactions
- Water and the fitness for biochemical reactions; the pH scale, acid dissociation constant of weak acids, buffered solutions resist changes in pH, low of mass action
- Amino acids and primary structures of proteins, some amino acid derivatives and non-protein amino acids
- Determination and identification of amino acids; spectrophotometric analysis, ninhydrin reaction mechanism, standard curve for determination
- Paper chromatography, thin layer chromatography, high voltage paper electrophoresis, HPLC, active charcoal, PVP
- Ammonium sulfate precipitation, dialysis
- Gel filtration chromatography
- Ion exchange chromatography, pI, DEAE, Q-sepharose, CM, SP, FPLC
- HIC (Hydrophobic interaction chromatography)
- Affinity chromatography
- GC (Gas chromatography)
- Purification of carbohydrates
- Purification of nucleic acids (PAGE)
| Midterm Exam(s)||1||20|
| Final Exam||1||40|
- On completion of the course, the students should be able to: Describe and compare different technologies for the purification of biomolecules
- Plan an efficient purification process for a biomolecule
- Carry out a chromatographic experiment to purify a biomolecule, calculate yield of the purification, and suggest improvements to reduce losses
- Write a scientific report on his experiment
- Critically review a report and constructively comment on the possibilities for improvements
- Reading list will be given each week of the courses. The course book will be complemented with descriptions from other literature and with relevant case studies from research.
|ECTS (Allocated based on student) WORKLOAD
|Lecture (14 weeks x Lecture hours per week)||14||3||42|
|Laboratory / Practice (14 weeks x Laboratory/Practice hours per week)|| || ||0|
|Midterm Examination (1 week)||1||2||2|
|Final Examination(1 week)||1||2||2|
|Preparation for Midterm Examination||1||25||25|
|Preparation for Final Examination||1||40||40|
|Assignment / Homework/ Project||14||3||42|
|Seminar / Presentation||1||3||3|