Master’s studies

Syllabus for Structure and Function of Proteins

Proteiners struktur och funktion


  • 10 credits
  • Course code: 1KB422
  • Education cycle: First cycle
  • Main field(s) of study and in-depth level: Chemistry G2F, Biology G2F
  • Grading system: Fail (U), 3, 4, 5
  • Established: 2016-03-10
  • Established by: The Faculty Board of Science and Technology
  • Revised: 2018-02-20
  • Revised by: The Faculty Board of Science and Technology
  • Applies from: week 30, 2018
  • Entry requirements: One of the following is required: (1) 60 credits of which at least 40 credits in chemistry including 15 credits in biochemistry, or (2) 60 credits of which at least 40 credits in biology, and 15 credits in biochemistry.
  • Responsible department: Department of Chemistry - BMC

Learning outcomes

After having completed the course, the students are expected to be able to :

  • describe mechanisms of cellular peptide/protein synthesis and degradation, major principles that govern protein folding and structure, and explain the fundamental connection between structure and function of proteins
  • describe different strategies and methods for the production, isolation, structure determination, functional analysis and modification of proteins
  • produce peptides and proteins and experimentally isolate and crystallize proteins as well as determine their basic physico-chemical and functional properties
  • analyse and interpret protein sequences and structures and use such information to predict protein function
  • describe how proteins can be used for production and development of drugs, for biotechnological and other industrial and scientific purposes, and explain how this is facilitated by knowledge of the structure and function of proteins
  • write a report in the form of a scientific article


Production and degradation: Biological and recombinant protein synthesis. Biological and chemical peptide synthesis. Post-translational and chemical modifications. Genetic engineering and directed evolution. Protein degradation.

Protein structure, function and bioinformatics: Folding. Structure determination by X-ray crystallography and NMR spectroscopy. Structure modelling and analysis using molecular graphics. Protein-ligand, protein-DNA and protein-protein interactions. Kinetic and thermodynamic characterisation of interactions. Examples for proteins: Enzymes, membrane proteins, structural proteins, regulatory proteins. Structure-function relationships. Introduction to databases for protein sequences, structures and functions and to protein bioinformatics tools and methods.

Applications: Examples for biotechnological, medical and scientific use of proteins.

Lab projects: Expression, purification, characterisation of an enzyme (the results of this project are presented in a report formed as a scientific publication). Protein crystallisation. Peptide synthesis.



The course is given in form of lectures as well as experimental and theoretical exercises and projects.
Exercises and projects are compulsory and carried out individually or in groups.


Experimental and theoretical exercises and projects (5 credits) are examined during the course. One of the reports should have a method section in English that meets the requirements set for publication in international journals in biochemistry. An overall written examination (5 credits) is given at the end of the course. The final grade for the course is given as a weighted average grade for all assessed parts.

Other directives

Cannot be included in a degree together with the course Structure and function of proteins 10 credits (1KB403).

Reading list

Reading list

Applies from: week 04, 2018

  • Whitford, David Proteins : structure and function

    Hoboken, N.J: Wiley, 2005

    Find in the library

  • Nelson, David L.; Cox, Michael M. Lehninger principles of biochemistry

    Seventh, international edition.: New York, NY: W.H. Freeman, [2017]

    Find in the library