The course is divided into a theoretical and a project part in order to give opportunity to deeper and more intergrated studies.The theory is presented and treated at lectures and lessons. Three-dimensional structures of proteins and computer simulations are performed in smaller groups. During the project part the students work with genetically mutated proteins cloned in bacteria. The origin of the mutated protein can be proteins that have been mutated by the students in an earlier course in gene technology or can be provided by the research group. The protein variants are characterized. Starting with a project plan the students perform the detail plans for the experimental work. This planning process will proceed interactively through meetings between the groups and the teacher/lab.assistant. The students should then independently evaluate their experimental results. The results of the experimental work is presented in a written report in english.
Theoretical part: Different structure motifs of proteins. Multifunctional enzymes, membrane proteins, prediction of protein structures. Studies of physico-chemical properties of proteins and methodology for studies of these properties: Chemical characteristics of polypeptides, protein engineering, physical interactions determining the properties of proteins, role of hydrophobic interaction, conformation flexibility, protein stability, mechanisms of protein folding, interaction with other proteins, enzyme catalysis.
Project part: Studies of physico-chemical properties of proteins and methodology for studies of these properties. Methodology used for these studies is biophysical methods such as fluorescence spectroscopy and CD. Sequence analysis and structure modeling are used for result analysis.
Responsible for this page: Lars-Göran Mårtensson
Last updated: 01/23/14