Analytical Biochemistry


After the course it is expected that the students know the biochemical and spectroscopic concepts needed to characterize biological systems at the structural and spectroscopic levels. With a strong experimental component, in an environment very similar to a research laboratory, it is intended that students:

  • develop the ability to understand and select appropriate techniques and methodologies in the study of a particular biological system
  • cultivate a critical analysis and interpretation, in an integrated manner, all experimental data

The writing and discussion of a final report seeks students to develop ability to write a scientific manuscript and acquire training in the critical review of the scientific literature and skills in presenting scientific papers.

General characterization





Responsible teacher

Carlos Alberto Gomes Salgueiro, Maria Alice Santos Pereira


Weekly - 4

Total - 60

Teaching language



Students should have attended the general courses of Biochemistry, Analytical Chemistry and Separation Methods and Molecular Biology taught in previous years.


  • Analytical biochemistry, 1998. ISBN-10: 058229438X
  • Bioanalytical chemistry, 2004. ISBN: 978-0-471-54447-0
  • Bioanalytical chemistry, 2004. ISBN-10: 1860943713
  • Physical biochemistry. Principles and applications, 2009. ISBN-10: 0470856033
  • Understanding bioanalytical chemistry. Principles and applications, 2009. ISBN-10: 0470029072

Teaching method

Teaching involves:

  1. Lectures taught using a "data-show", accompanied by supplementary bibliography previously available on the course page in CLIP. In the first class of the semester all information about the curricular unit will be presented. Evaluation will be discussed as well.
  1. Problem-solving sessions, putting in practice the theoretical concepts acquired throughout the different classes.
  2. Laboratory sessions with groups of four students, where students conduct experimental work following laboratory protocols previously distributed to all students. 

All the information about the course is accessible through the dedicated web page on CLIP platform. In this site all pdfs files of the lectures presentations, laboratory protocols and exercises will be available.

Evaluation method

Students will be admitted to evalutaion of the theoretical component with frequency.

The frequency is obtained by:

  • compulsory attendance of all laboratory sessions
  • delivery of the laboratory report (1/group)

Evaluation of the practical component:

  • Punctuality, preparation and execution of laboratory classes
    • delays to laboratory classes or non-preparation will contribute -0.5 values to the final grade of the practical component
  • Evaluation of the laboratory report

The assessment of the theoretical component:

Will be carried out by performing three theoretical tests, with a contribution of 45%, 40% and 15%, respectively.

Final grade:

40% practical component + 60% theoretical componente


  • Approval to the curricular unit requires a final grade 9.5 in each of the components, theoretical and practical.
  • All scores (tests and evaluation of the practical component) will be rounded to the tenth.
  • On appeal exam (recurso or other) only the theoretical component will be evaluated.
  • Improvement of the final grade will contemplate only the theoretical component.


Subject matter

The syllabus of this curricular unit:

1.   Analysis and quantification of biomolecules

1.1.   Major methods to detect and quantify biomolecule
1.2.   Qualitative versus quantitative analyses
1.3.   Parameters used in the identifiation and quantification of biomolecules

2.   Extraction and purification of proteins - special cases

2.1.   Experimental strategies versus aim of the target
2.2.   Recombinant proteíns
2.3.   Overexpression of recombinant membrane proteins

3.   Analysis of carbohydrates

3.1.   Chemical and enzymatic methods to identify and quantify carbohydrates
3.2.   Separation of a complex mixture of carbohydrates

4.   Analysis of lipids

4.1.   Sample preparation
4.2.   Quantitative methods
4.3.   Separation of complex mixtures of lipids

5.   Immunological methods

5.1.   Antibody-antigene interaction
5.2.   Analyticla aplication of biological markers
5.3.   Applications of immunological methods

6.   Mass spectromety

6.1.   Theoretica concepts
6.2.   Tandem mass spectrometry
6.3.   Applications

7.   Bioanalysis of proteins by Nuclear magnetic Resonance spectroscopy

7.1.   Theoretical concepts
7.2.   Mono- and multidimensional NMR
7.3.   Isotopic enrichment of proteins to be studied by NMR
7.4.   Applications to biological systems

8.   Protein folding

8.1.   Thermodynamics of the denaturation process
8.2.   Stability curves: effect of the temperature
8.3.   Mechanisms of folding
8.4.   Diseases associated to protein unfolding


Programs where the course is taught: