BMB533: Molecular biology and protein chemistry (10 ECTS)

STADS: 01011001

Level
Bachelor course

Teaching period
The course is offered in the autumn semester.

Teacher responsible
Email: srd@bmb.sdu.dk

Additional teachers
larsgr@bmb.sdu.dk
ihk@bmb.sdu.dk
jens.andersen@bmb.sdu.dk

Timetable
Group Type Day Time Classroom Weeks Comment
Common I Monday 08-10 U140 49
Common I Monday 12-14 U140 50-51
Common I Tuesday 14-16 U140 36,38
Common I Thursday 14-16 U55 37-41,43-48
Common I Friday 08-10 U55 36
Common I Friday 15-17 U140 37
H1 TL Tuesday 10-12 White Lab 44
H1 TE Wednesday 12-14 U145 36-41,43-51
H1 TL Friday 08-10 White Lab 40-41
H1 TL Friday 14-16 White Lab 43
H2 TE Thursday 08-10 U81 36-41,43-51
H2 TL Thursday 12-14 White Lab 40,43
H2 TL Thursday 16-18 White Lab 41,44
H3 TE Tuesday 16-18 U145 36,38
H3 TE Tuesday 14-16 U145 37,39-41,43,45-51
H3 TL Wednesday 10-12 White Lab 40-41,43-44
H3 TE Thursday 12-14 U105 44
H4 TL Wednesday 12-14 White Lab 40-41,43-44
H4 TE Wednesday 14-16 U156 44
H4 TE Friday 12-14 U145 36-41,43,45-51
H5 TL Monday 08-10 White Lab 40-41,43-44
H5 TE Thursday 12-14 U133 40
H5 TE Friday 10-12 U141 36-38,41,43-51
H5 TE Friday 14-16 U151 39
H6 TE Monday 14-16 U141 37-41,43-51
H6 TL Monday 10-12 White Lab 40-41,43-44
H6 TE Thursday 10-12 U145 36
Show entire timetable
Show personal time table for this course.

Prerequisites:
None

Academic preconditions:
Material FF503 or equivalent presumed known.

Course introduction
The course aims to give a general introduction to the molecular biology of prokaryotes and eukaryotes. Students will learn about the structure of biological macromolecules involved in the flow of genetic information (DNA, RNA and proteins) as well as their functions in the storage and transfer of genetic information in living cells. The course gives the basic knowledge that is necessary for the more advanced courses in molecular biology. In addition an introduction will be given to the structure and function of proteins and how they work in a cellular and physiological context through interactions with proteins and other biomolecules.

Qualifications
Students will gain a broad insight into the fields of molecular biology and protein chemistry, and will learn how to use this knowledge, for example:

  • to understand scientific questions and terms within molecular biology’s and protein chemistry’s central disciplines
  • to understand how genetic information is conveyed within all living cells, according to the central dogma of molecular biology
  • to be able to express oneself using precise scientific and technical terminology
  • to be able to understand and evaluate information concerning molecular biology and protein chemistry that is presented in the media and scientific literature
Expected learning outcome
After completing the course, students will be able to:

  • Define common terms within genetics and molecular biology
  • Explain the flow of genetic information from gene to protein (the central dogma)
  • Explain the connection between structure and function of nucleic acids
  • Describe the basic steps in replication, transcription and translation
  • Outline the composition of the enzyme complexes associated with replication, transcription and translation
  • Outline the principles behind regulation of the genetic flow at the DNA, RNA and protein level
  • Describe examples of regulation of gene expression at the DNA, RNA and protein levels
  • Describe the significant differences between gene expression in eukaryotes and prokaryotes
  • Outline the mechanisms of homolog and non-homolog recombination
  • Outline mechanisms of gene mutation and their significance at the molecular, cellular and organism level
  • Know the principles of the common techniques employed in molecular biology and gene technology
  • Draw the chemical structure of the twenty amino acids and their modifications to the structure and function of proteins
  • Classify the primary, secondary, tertiary and quaternary level of protein structure
  • Use the program VMD to visualize the tertiary structure of proteins and use this tool to address structural problems
  • Use the program Cytoscape for visualization of protein-protein interaction data
  • Describe how cellular proteins are folded, misfolded and degraded, and how errors in these processes can give rise to disease
  • Know about modern protein chemistry techniques for purification, characterization and bioinformatical analysis of proteins
  • Describe how proteins function together with other biomolecules in cellular and physiological contexts including the immune system, blood coagulation and sensory and motoric systems
  • Conduct independent a literature search to discuss a selected protein chemistry topic from a molecular biological perspective
Subject overview
Protein structure and folding
Protein structure and function
The function of proteins in a physiological context
Posttranslational modification of proteins
Protein degradation
Methods in protein chemistry
Information flow from gene to protein
Genome organization in pro- and eukaryotes
Structure and function of nucleic acids (DNA and RNA)
Replication of DNA, including regulation of DNA synthesis
Mechanisms of DNA recombination
Mutation of DNA and its repair
Mechanisms of transposition
Synthesis of RNA by transcription from DNA
Regulation of gene expression
Processing of RNA including splicing of mRNA
Ribosome’s structure functions in protein synthesis
Protein localization and export
Proteins involved in the control of the cell cycle
Antibiotics and cytotoxins
Fundamental techniques within molecular biology including PCR, DNA sequencing, gene cloning etc.

Literature
  • Berg, Tymoczko og Stryer: Biochemistry, 7. udgave. Ekstra materiale vil blive udvalgt fra år til år.


Website
This course uses e-learn (blackboard).

Prerequisites for participating in the exam
  1. Approved assignments, evaluated by internal censorship on a pass/fail basis. It will be possible to a re-hand in of one of the total number of assignments (01011012)
Assessment and marking:
  1. 4 hours written examination. Written aids in paper version are allowed, while electronic aids are not. Evaluated by external censorship by the 7-mark scale (10 ECTS). (01011002)
Expected working hours
The teaching method is based on three phase model.
Intro phase: 40 hours
Skills training phase: 38 hours, hereof:
 - Tutorials: 28 hours
 - Laboratory exercises: 10 hours

Educational activities Study phase: 130 hours

Language
This course is taught in Danish or English, depending on the lecturer. However, if international students participate, the teaching language will always be English.

Course enrollment
See deadline of enrolment.

Tuition fees for single courses
See fees for single courses.