Course syllabus

Course-PM

KBB058 Structure and dynamics of biomolecules lp2 HT19 (7.5 hp)

Course is offered by the Department of Chemistry and Molecular Biology, University of Gothenburg.

Contact details

Course responsible:

Gergely Katona gergely.katona@gu.se, Lundberg Laboratory

Teachers:

MB = Martin Billeter, martin.billeter@gu.se

BB = Björn Burman, bjorn.burman@gu.se

VO = Vladislav Orekhov, vladislav.orekhov@gu.se

RN = Richard Neutze, richard.neutze@chem.gu.se

JH = Johanna Höög, johanna.hoog@gu.se

GK = Gergely Katona, gergely.katona@gu.se

GB = Gisela Bränden, gisela.branden@gu.se

FS = Florian Schmitz, florian.schmitz@gu.se

VA = Viktor Ahlberg Gagner, viktor.ahlberg.gagner@gu.se

DZ = Davide Zabeo, davide.zabeo@gu.se

JC = Jacob Croft, jacob.croft@gu.se

Course purpose

Short description of the course purpose and content: can be copied from syllabus in Studieportalen. Additional information can be added.

Schedule

Most up to date schedule is in the pdf document, the KBB058 course is marked with white and blue items, participation in the green items is optional and does not give extra credit:

KEM360_schedule_2019_final.pdf

TimeEdit

Course literature

General overview of the techniques: 

Methods in Molecular Biophysics Nathan R. Zaccai, Igor N. Serdyuk, Joseph Zaccai  Cambridge University Press (2017) ISBN: 9781107056374

Recommended chapters: Part E, Part F2-2.6.5, Part G, Part H, Part J

Further readings:

X-ray crystallography: Crystallography Made Crystal Clear: A Guide for Users of Macromolecular Models. Gale Rhodes, Academic Press (2006) ISBN:978-0-12-587073-3

Recommended chapters: 3-9

General overview of the techniques: Wilson, Keith (Ed.). (2010). Principles and techniques of biochemistry and molecular biology. (7. ed.). Cambridge: Cambridge University Press. ISBN: 9780521731676

Recommended chapters: 8.3, 13.1-2, 13.4-8, 18.2-18.3

Course design

The course has theoretical lecture series covering the main techniques used for biological structure determination: X-ray crystallography, NMR spectroscopy, electron microscopy and small angle X-ray scattering.  A lecture and a practical linked to the mathematical background connecting these techniques together.  The content of the lectures are evaluated by a written exam at the end of the course.

The laboratories include wet lab and practical work which includes protein crystallization and sample preparation for electron microscopy. The remaining laboratories are computer based and illustrate X-ray crystallographic and NMR data processing and structural analysis.  During the practicals the students are actively involved in designing their experiment and setting the research goals. The laboratories are compulsory and the laboratory reports are required for passing that part of the course. It is possible to revise a laboratory report one time.

Changes made since the last occasion

A summary of changes made since the last occasion.

Learning objectives and syllabus

Learning objectives:

The course provides advanced knowledge of the methods for studying biomolecular structure and dynamical properties (X-ray diffraction of protein crystals, nuclear magnetic resonance and electron microscopy) and the molecular interplay between biomolecules (DNA - protein-ligand interactions).

It also deals with the theory and basic mathematical concepts (Fourier transform) for spectroscopic and X-ray scattering methods in biology and biochemistry. The course also provides an in-depth knowledge of the biochemical methodology and an understanding how structure and function is linked in biological molecules. In relevant context protein structure-based drug design is discussed.

The theoretical and practical parts lie close to the current research and are designed to prepare graduates for a degree in biochemistry or for post graduate studies in the subject.

After completing the course, the students will be able to:

  • explain biomolecular structure and dynamics
  • be familiar with modern biophysics and biomolecular structure research
  • critically assess the potential and limitations of different experimental methods
  • have a deeper understanding of protein structure-function relationship.
  • have knowledge about and be able to apply the methods of crystallization, X-ray diffraction data collection of both soluble and membrane-bound proteins
  • be informed about, and to some extent able to apply NMR methods for characterization of proteins and their interactions
  • possess the practical knowledge necessary for the characterization of proteins and determine their three-dimensional structure
  • describe different analysis tools such as molecular graphics and Fourier transformation
  • interpret and discuss laboratory results and draw reasonable conclusions
  • critically, independently and creatively analyze the structure and function of a protein, implementing these advanced tasks within specified time frames
  • demonstrate an ability to both national and international contexts, orally and in writing present and discuss their conclusions

Course syllabus can be found at http://kursplaner.gu.se/pdf/kurs/sv/KEM360Links to an external site. and http://kursplaner.gu.se/pdf/kurs/en/KEM360Links to an external site. for an english version.

Study plan

Examination form

 The content of the lectures are evaluated by a written exam at the end of the course. The laboratories are compulsory and the laboratory reports are required for passing that part of the course. 

Course summary:

Date Details