Course syllabus

Jump to today

Course-PM

BBT005 Protein folding and function lp3 VT20 (7.5 hp)

Course is offered by the department of Biology and Biological Engineering

Contact details

Examiner and Course organisation:
Elin Esbjörner Winters
eline@chalmers.se
phone: 031-7725120
Room: 2052B (Chemistry research building I, floor 5)

Lecturers:
Elin Esbjörner Winters (see above for contact details)
Sandra Rocha (sandra.rocha@chalmers.se)
Pernilla Wittung-Stafshede (pernilla.wittung@chalmers.se)
Ranjeet Kumar (ranjeet@chalmers.se)

Lab project supervisor:
Nima Sasanian (sasanian@chalmers.se)
Ranjeet Kumar (ranjeet@chalmers.se)

Course purpose

This course aims to provide students with extensive practical and theoretical knowledge of protein biophysics, focusing on their folding, misfolding, and function. The course focuses on theories, practices and concepts that are used in contemporary academic and industrial research and is preparatory for PhD studies as well as for research-oriented jobs in the industrial sector.

Schedule

TimeEdit
The course follows the pdf-schedule handed out at beginning of course. This schedule overrules that in time edit.

Course literature

The course literature consists of handed-out material in the form of research and review papers and book chapters. All course material will be available in Canvas (as pdf files).

Course design

The course consists of a blend of lectures, problem-solving sessions (self-study based, teacher available, intended to prepare students to independently solve problems), a  lecture-integrated literature assignment and a lab project (1-2 days). The literature assignment is designed to integrate active learning moments and the purpose of the lab project is for the students to  apply theoretical knowledge in practice as well as to learn how to operate instruments that are common in protein research.

The course content and lectures are organized in Canvas.
Students are encouraged to contact teachers via email stating the course code (BBT005) in the subject line.

Changes made since the last occasion

Introductory lecture have been condensed and aligned to avoid too much repetition (between lectures and from previous courses).

Part on protein purification has been extended.

Booklet with problem-solving exercises updated.

Fewer lecturers involved in the course.

Lab projects developed (due to increasing number of course participants)

Learning objectives and syllabus

Learning objectives:

  • describe and understand the thermodynamic stability of proteins. Be able to apply this knowledge to interpret experimental data and calculate thermodynamic parameters for proteins with different mechanisms of folding.
  • describe the energy landscape of protein folding and misfolding from a thermodynamic point of view.
  • understand and describe theoretical models for protein folding kinetics and amyloid formation. Be able to use this knowledge to interpret experimental data and model folding kinetics.
  • understand and describe the theoretical foundation of and applied aspects of common and modern protein biopysics techniques. Be able to use this knowledge to evaluate and interpret own experimental data as well as to understand the scientific literature in this area.
  • be able to suggest and evaluate experimental strategies for protein biophysics investigations in order to independently plan experiments to characterise a protein's thermodynamic stability, folding kinetics, and function.
  • describe amyloid fibril structure and biophysical properties and become familiar with the relationship between protein misfolding and amyloid formation and neurodegenerative disease.
  • obtain knowledge of and understand different biophysical and biochemical methods for the detection and analysis of protein aggregates. Be able to use this knowledge to study protein aggregation and amyloid formation in vitro and acquire a basic understanding of corresponding methodologies and practises to detect protein aggregates in biological samples.
  • become familiar with the fundamental principles of protein folding and stability in vivo in order to be able to describe how a protein's properties are affected by different cellular processes.
  • acquire knowledge of different methods for fluorescent labelling of proteins and knowledge of their advantages and shortcomings. Be able to use this knowledge to independently suggest how to design fluorescently labelled proteins to enable folding and interaction studies in vitro and in vivo.
  • become able to search, read, critically evaluate and discuss scientific literature related to protein folding, misfolding, stability and function.

https://student.portal.chalmers.se/en/chalmersstudies/courseinformation/Pages/SearchCourse.aspx?course_id=29923&parsergrp=3

Study plan

Examination form

Requirements to pass the course:

  1. Approved written exam (grade 3 or higher).
  2. Approved literature assignment (brief essay + oral presentation)
  3. Performed and presented laboratory mini project

The examination is described in detail in the course-PM

 

Course summary:

Date Details Due