BMB533: Molecular biology and protein chemistry

• Have a basic knowledge of physics, chemistry and biology


• Be able to use a computer and access the internet

The course builds on the subject matter covered in the courses FF503 and BMB531, and gives an academic basis for understanding the topics in the later courses BMB507 and BMB508.

In relation to the competence profile of the degree it is the explicit focus of the course to:

• Give competence in understanding the terminology used in molecular biology and protein chemistry.


• Give skills to express yourself clearly in the language used in these disciplines.


• Give knowledge and understanding of the flow of genetic information in all cells.


• Give the competence to understand and critically evaluate information relating to the fields of molecular biology and protein chemistry, when these are reported in scientific journals and in the media.

• Know how to use correctly general terminology within the fields of genetics, molecular biology and protein chemistry.


• Explain the Central Dogma of the flow of information from genes to proteins.


• Explain connection between nucleic acid structure and function in the Central Dogma information flow.  


• Describe the basic steps in DNA replication and transcription, and mRNA translation to proteins.


• Describe the combinations of enzyme complexes that are involved in DNA replication and transcription, and mRNA translation to proteins.


• Understand the principles of gene regulation.


• Give detailed, specific examples of these processes. 


• Distinguish the differences between the molecular processes governing these processes in prokaryotes and eukaryotes.


• Sketch the mechanisms involved in homologous and specific recombination.


• List the main causes of mutation and the consequences of these at the molecular and cellular levels and their potential effects on the whole organism.


• Demonstrate knowledge of general techniques in molecular biology and gene technology.  


• Describe the chemical structures of the twenty common amino acids, and how modification of these alters protein structure and function.


• Differentiate between primary, secondary and tertiary structures of proteins and describe quaternary interactions within protein complexes.


• Use the programs VMD and Cytoscape for visualizing macromolecular structures, and its application in discovering details of molecular interactions.  


• Describe the folding, misfolding and degradation of proteins, and how deviations in these molecular pathways can lead to disease.


• Attain knowledge of modern methodology in protein chemistry, protein purification, characterization and their analysis using bioinformatics. 


• Demonstrate knowledge of how proteins interaction with other biological macromolecules during the execution of physiological processes in the cell. This includes an understanding of how proteins function in the immune system, in blood clotting, and in sensory and motoric systems. 


• Independently search and find relevant information to answer questions concerning the topics covered on this course.

• Protein structure, folding and function


• Protein function in the context of physiology 


• Post translational modification of proteins


• Protein degradation 


• Methods in protein chemistry


• Genome organization in prokaryotes and eukaryotes


• Information flow from gene to protein 


• Structure and function of nucleic acids (DNA og RNA)


• DNA replication, including regulation of DNA synthesis


• Mechanisms of DNA recombination 


• Mutations and repair of DNA


• Mechanisms of transposition 


• Synthesis of RNA via DNA transcription


• Regulation of gene expression


• RNA processing and mRNA splicing


• Composition of ribosomes and their function in protein synthesis


• Protein localization and export


• Control of the cell cycle by proteins 


• Antibiotics and cytotoxins


• Fundamental metods used in molecular biology, including PCR, DNA sequencing, gene cloning.

• Berg, Tymoczko og Stryer: Biochemistry, 8. ed.
• Additional material will be selected from year to year.

See Blackboard for syllabus lists and additional literature references.

• Tutorials: 30 hours
  
• Laboratory exercises: 8 hours
  

• Study text book, slides from the lectures


• Write and read notes, work on the exercises.