Course syllabus for Protein folding and function

Course syllabus adopted 2020-02-05 by Head of Programme (or corresponding).

Overview

  • Swedish nameProteiners veckning och funktion
  • CodeBBT005
  • Credits7.5 Credits
  • OwnerMPBIO
  • Education cycleSecond-cycle
  • Main field of studyBioengineering
  • DepartmentLIFE SCIENCES
  • GradingTH - Pass with distinction (5), Pass with credit (4), Pass (3), Fail

Course round 1

  • Teaching language English
  • Application code 08131
  • Maximum participants30
  • Open for exchange studentsYes

Credit distribution

0116 Examination 4.5 c
Grading: TH		 4.5 c
  • 20 Mar 2021 am J
  • 10 Jun 2021 am J
  • 18 Aug 2021 am J
0216 Written and oral assignments 1.5 c
Grading: UG		 1.5 c
0316 Laboratory 1.5 c
Grading: UG		 1.5 c

In programmes

Examiner

Go to coursepage (Opens in new tab)

Eligibility

General entry requirements for Master's level (second cycle)
Applicants enrolled in a programme at Chalmers where the course is included in the study programme are exempted from fulfilling the requirements above.

Specific entry requirements

English 6 (or by other approved means with the equivalent proficiency level)
Applicants enrolled in a programme at Chalmers where the course is included in the study programme are exempted from fulfilling the requirements above.

Course specific prerequisites

General knowledge of chemistry, including physical chemistry and biochemistry

Aim

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.

Learning outcomes (after completion of the course the student should be able to)

  • 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.

Content

Fundamental biophysical properties of proteins, the energy landscape for protein folding and misfolding, biophysical and biochemical methods for proteins, thermodynamic stability, folding kinetics, amyloid fibrils: structure and kinetics, fluorescence labelling of proteins, chaperones, protein-protein and protein-ligand interactions, metalloproteins, proteins in vivo.

Organisation

Lectures and tutorials, literature assignments with written report, experimental project with oral and written examination.

Literature

The course will be taught based on scientific literature, using original research articles as well as review papers in combination with a course compendium.

Examination including compulsory elements

Written exam, approved literature report, approved project report and oral presentation.