INTERNATIONAL BURCH UNIVERSITY
Graduate Study - Faculty of Engineering and Natural Sciences
Genetics and Bioengineering Master With Thesis
2013-2014

SYLLABUS
Code Name Level Year Semester
GBE 513 Purification Techniques of Biomolecules Graduate 1 Spring
Status Number of ECTS Credits Class Hours Per Week Total Hours Per Semester Language
Non-area Elective 7.5 3 216 English

Instructor Assistant Coordinator
, Yusuf Turan, Prof. Dr.
no email no email

COURSE OBJECTIVE
The objective of the course is to provide a general overview of bioseparation processes starting from a raw material and all the way through to a final product giving basic knowledge of physico-chemical principles behind different methods of separation of biomolecules. A technical aspect will also be covered, including standard and advanced techniques of biomolecules analysis, extraction and purification, with a special focus on proteins purification. An important part of the course is the presentation of the case study.

COURSE CONTENT
Week
Topic
  1. Biomolecules structure, physical and chemical characteristics
  2. Function and interactions of biomolecules in the cell
  3. Breaking of the cell by physical and chemical methods, fractionation methods, protein concentration
  4. Centrifugation basic principles, preparative and analytical, types of centrifuges and rotors. Preparative ultracentrifugation, differential centrifugation, density-gradient, analytical ultracentrifugation and applications in determination of molecular weight, purity and detection of conformational changes in macromolecules.
  5. Electrophoretics techniques, basic principles, electrophoresis of proteins, nucleic acids. PAGE–Native PAGE, SDS-PAGE, Isoelectricfocussing, 2D electrophoresis, identification of novel proteins in 2D gels, capillary electrophoresis. Agarose gel electrophoresis
  6. Electrophoretics techniques, basic principles, electrophoresis of proteins, nucleic acids. PAGE–Native PAGE, SDS-PAGE, Isoelectricfocussing, 2D electrophoresis, identification of novel proteins in 2D gels, capillary electrophoresis. Agarose gel electrophoresis
  7. Electrophoretics techniques, basic principles, electrophoresis of proteins, nucleic acids. PAGE–Native PAGE, SDS-PAGE, Isoelectricfocussing, 2D electrophoresis, identification of novel proteins in 2D gels, capillary electrophoresis. Agarose gel electrophoresis
  8. Chromatographic techniques. Principles, instrumentation and applications of thin layer and gas chromatography. Column chromatography-packing, loading, eluting and detection. Ion-exchange chromatography preparation of resins, procedure and applications. Molecular exclusion chromatography-principle, gel preparation, operation and applications. Affinity chromatography–principle, materials, procedure and applications. Special forms of affinity chromatography– immunoaffinity, metal chelate, dye-ligand and coval

  1. Chromatographic techniques. Principles, instrumentation and applications of thin layer and gas chromatography. Column chromatography-packing, loading, eluting and detection. Ion-exchange chromatography preparation of resins, procedure and applications. Molecular exclusion chromatography-principle, gel preparation, operation and applications. Affinity chromatography–principle, materials, procedure and applications. Special forms of affinity chromatography– immunoaffinity, metal chelate, dye-ligand and coval
  2. Chromatographic techniques. Principles, instrumentation and applications of thin layer and gas chromatography. Column chromatography-packing, loading, eluting and detection. Ion-exchange chromatography preparation of resins, procedure and applications. Molecular exclusion chromatography-principle, gel preparation, operation and applications. Affinity chromatography–principle, materials, procedure and applications. Special forms of affinity chromatography– immunoaffinity, metal chelate, dye-ligand and coval
  3. Protein structure, purification and characteristics.
  4. Spectrophotometrical methods for protein analysis Theory, different techniques, applications.
  5. Case study
  6. Discussion on course material, exam prep.

LABORATORY/PRACTICE PLAN
Week
Topic

    TEACHING/ASSESSMENT
    Description
    • Lectures
    • Presentation
    • Case Studies
    • Demonstration
    Description (%)
    Method Quantity Percentage (%)
    Homework30
    Midterm Exam(s)30
    Final Exam140
    Total: 100
    Learning outcomes
    • - be able to describe the basic structure of bioseparation process from a raw material and all the way through to a final product
    • − be able to describe different methods for protein purification, their properties, advantages/disadvantages and when they should be used.
    • − describe different protein analysis methods, their properties, advantages/disadvantages and when they should be used.
    • − plan a functional purification scheme for a protein.
    • − be able to independently design a method for separation and purification of propsed biomolecule from raw material
    TEXTBOOK(S)
    • Principles and Techniques of Biochemistry and Molecular Biology (2005) by Keith Wilson and John Walker, (ISBN-13: 978052151639858

    ECTS (Allocated based on student) WORKLOAD
    Activities Quantity Duration (Hour) Total Work Load
    Lecture (14 weeks x Lecture hours per week)348144
    Laboratory / Practice (14 weeks x Laboratory/Practice hours per week)23264
    Midterm Examination (1 week)224
    Final Examination(1 week)224
    Preparation for Midterm Examination 0
    Preparation for Final Examination50
    Total Workload: 216
    ECTS Credit (Total workload/25): 9