Biophysical Methods & Structural Biology (2026/2027: Periode 1)

Bekijk rooster Print deze pagina

Cursusdoel

Upon successful completion of this course, students will be able to:
  1. Describe the basic principles of the experimental methods treated in the course, i.e. light microscopy, EM, MS, NMR, and XRD.
  2. Identify the appropriate experimental methods for a given research question;
  3. Critically assess the outcome of a quantitative data analysis;
  4. Search, access, view and evaluate atomic models of biomolecules with common database search tools and software packages;
  5. Assimilate biophysical and structural data from multiple methods to formulate molecular mechanisms and models of biomolecular organization;
  6. Analyse, perform literature searches and report on the biomolecular organization of a biological system;
  7. Effectively work collaboratively in a group assignment with their peers and reflect on their role in this collaboration.

Vakinhoudelijk

In this course students study the basic principles underlying biophysical and structural biology methods such as light and electron microscopy and different forms of spectroscopy. Students practice with real data and in doing so, learn how to interpret the quality of quantitative data based on key figures-of-merit and how this quality relates to the biological information that can be extracted from the data.

Set up of this course: In this course plenary lectures, group work, and individual computer practicals all contribute to a deep learning experience aimed at familiarizing students with the theory behind, and applications of, microscopy and spectroscopy in structural biology. One aspect all techniques have in common is that data analysis is a crucial step in the experimentation process. A theoretical basis for the retrieval of useful biological information from primary measurements and the assessment of data quality and information content is laid down in the plenary lectures.

In a series of context-rich lectures key insights into the molecular organization of life that these methods have brought us are discussed. In these lectures experimental challenges for microscopy and spectroscopy, other than data analyses, are covered (determining the structure and organisation of biological complexes; imaging live tissues and cells on relevant timescales; identifying biomolecules in a cellular context at the nanometer scale; uncovering biological interaction networks at a systems-wide scale.)

Information from the lectures is practiced and applied in weekly tutorials and several computer practicals

Throughout the course, students work on a case study about the biomolecular organization of a biological system of their choice. In this group assignment students explore this biological system by analysing and reviewing published literature (journal club style) and by retrieving and exploring molecular models from databases. In the final weeks of the course, students prepare a presentation to explain to their fellow students how various biophysical and structural biology methods were essential in providing the original researchers key insights into the molecular organization of their chosen system.

Relation to other courses: This course builds on (1) mathematical and programming skills introduced in MBLS-102 ‘Mathematics and Programming’ and applied in MBLS-106 ‘Biological Physics’, and on (2) MBLS-104 ‘Physical Chemistry for the Life Sciences’ in which basic concepts of NMR and MS are introduced. This course prepares students for the following level 2 and 3 courses ‘Advanced Structural Biology', ‘NMR spectroscopy and Molecular modelling’, ‘Mass Spectrometry and Proteomics’, and ‘Light and Electron Microscopy’.

Teaching formats course (estimation):
In this course lectures are alternated with computer practicals and tutorials. A context-rich group assignment is used to integrate the various aspects of this course in a final project.

Lectures = 60%
Tutorials (werkcolleges) = 25%
Practicals = 10%
Presenting = 5%

Grading (see course manual for details):

  1. Exam 1 (40%)
  2. Exam 2 (40%)
  3. Case study report & presentation (20%)

Participation in the computer practicals is required for admittance to the written exams.
The minimum grade required to pass the course is a 5 for each component (2 exams and the group presentation), with a weighted average score of at least 5.5.

Werkvormen

Computerpracticum

Hoorcollege

Werkcollege

Toetsing

Eindresultaat

Verplicht | Weging 100% | ECTS 7,5

Ingangseisen en voorkennis

Ingangseisen

Je moet inschreven staan voor een van de volgende opleidingen:

  • Molecular and Biophysical Life Sciences
  • Scheikunde

Voorkennis

This course is open for bachelor students Chemistry. For MBLS and Chemistry students successful completion of MBLS-105 or SK-B1BMC (Biomolecular Chemistry), basic knowledge about NMR and Mass Spectrometry (MBLS-104, spectroscopy part), and Mathematics & Python programming (MBLS-102), or demonstrable equivalent pre-knowledge and skills are highly recommended.

Voertalen

  • Engels

Cursusmomenten

Gerelateerde studies

Tentamens

Er is geen tentamenrooster beschikbaar voor deze cursus

Verplicht materiaal

  • READER
    Course syllabus Biophysical Methods and Structural Biology.
  • SOFTWARE
    Python (open source)
  • SOFTWARE
    ChimeraX (open source)

Aanbevolen materiaal

Er is geen informatie over de aanbevolen literatuur bekend

Coördinator

dr. J. Snijder J.Snijder@uu.nl

Docenten

dr. J. Snijder J.Snijder@uu.nl
dr. S.C. Howes s.c.howes@uu.nl
dr. H. van Ingen H.vanIngen@uu.nl
prof. dr. L.C. Kapitein l.kapitein@uu.nl

Inschrijving

Let op: deze cursus is niet toegankelijk voor studenten van andere faculteiten, bijvakkers mogen zich dus niet inschrijven.

Naar OSIRIS-inschrijvingen
Permanente link naar de cursuspagina
Laat in de Cursus-Catalogus zien