Stockholm university
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Analytical Chemistry, Bioanalytical Chemistry

The course provides an overview of genomics and proteomics. The course aims to provide knowledge about biomolecules and bioanalytical methods.

It will also give a deeper understanding of strategies for the development of analytical methods and sampling methodology and handling of biological matrices. A broad interdisciplinary exposure is achieved with emphasis on critical thinking. The course goes beyond learning techniques for their own sake but enabling students to determine the best methods for the appropriate biological questions to be addressed as well as a general ability to grasp key issues in the life and environmental sciences.

  • Course structure

    The course consists of lectures, workshops/demos, laboratory project work, oral and written presentation of scientific work within the field of bioanalytical chemistry with aspects as follows:

    Chromatography: Biomolecular applications of basics learned from the previous separation course that covers Liquid Chromatography (Including Reversed- and Normal Phase LC, Ion Chromatography, Size Exclusion Chromatography) Preparative Chromatography etc will be explored.

    Mass spectrometry: Focus on biological mass spectrometry from small molecules to lipids, carbohydrates, proteins and their complexes. Native mass spectrometry extends the familiar notions of learned in previous courses thus going beyond introductory LC/MS and MS/MS.

    Guest lectures: in order to keep up with the wide breadth of bioanalytical chemistry, there will be guest lectures that cover the latest research given by experts in the fields of: proteomics, metabolomics, new mass spectrometric methods, spectroscopy, novel separation methods, chemical ecology and native mass spectrometry

    Problem Based Learning: This revolves around the emerging toxin BMAA and its isomers. We trace its history and the impact analytical chemistry has played a role in the proper investigation of this simple yet enigmatic non-proteinogenic amino acid. Methods, strategies and the general analytical thinking involved in the unravelling the properties and activities of these compounds allows for training the bioanalytical chemist in how to approach challenging questions in the life and environmental sciences.

    Project work: Literature and Experimental Projects -  Project Planning, Risk Assessment, Method Development, Experimental Work, Oral presentation and Report Writing, Documentation and Good Laboratory Practice (GLP), Method validation.

    Experimental Work

    Through the different laboratory exercises, students are introduced and familiarized with the concept of peptide mapping by performing both HPLC-UV and MALDI-ToF analysis of tryptic digests.

    During these exercises they obtain experience on all the steps of the analytical procedure, including sample preparation, analysis, as well as data evaluation using suitable data base search.

    They are also trained on planning experiments using information from a scientific article, in order to perform similar experiments.

    The purpose of the laboratory exercises is to familiarize students with the sample preparation techniques and instrumentation commonly used in bioanalysis. The students have also chance to learn how to perform protein identification with help of databases and Mass Spectrometry.

    The students also have a chance to learn how to perform protein identification with help of databases and Mass Spectrometry.
    The course is concluded by the project work that students plan and perform independently. The project allows the students to creatively use the knowledge gained during the Bioanalytical Chemistry course and obtain experience with analytical equipment and instrumentation.

    Special demonstrations on advanced instrumentations will also be carried out. Of particular special interest is on the growing field of native mass spectrometry. Analyses of peptides and intact proteins/assemblies are increasingly important as protein based drugs are growing targets of pharmaceutical industries. Practicals on the analyses of neurotoxins that constitute the bulk of problem based learning exercises will also be explored.


    Theory 7.5 ETCS

    Laboratory 7.5 ETCS

    Teaching format

    The theoretical part includes

    • lectures
    • homework assignments
    • group work
    • peer-review
    • seminars


    In order to pass the course you have to pass the written examination (i.e. mark E or higher) as well as pass the oral and written presentations of the labs and project.

    Written exam, graded A-F.

    Project report and project work performance are graded as PASS/FAIL

    Completion of all project reports on time generally accrues bonus points as well as other advanced tasks.

    However, these are all subject to change from year to year.


    Docent Leopold L. Ilag


  • Schedule

    The schedule will be available no later than one month before the start of the course. We do not recommend print-outs as changes can occur. At the start of the course, your department will advise where you can find your schedule during the course.
  • Course literature

    Note that the course literature can be changed up to two months before the start of the course.

    Most literature are based on journal articles although a general book which serves as a good reference is a book by Gary Siuzdak,

    The Expanding Role of Mass Spectrometry in Biotechnology found online here

  • Course reports

  • Contact

    Course responsible:

    Docent Leopold L. Ilag


    Chemistry Section & Student Affairs Office:

    Office:        Chemical Practice Laboratory M345