spring 2016
KJE-8701 BIOSTRUCT - Biophysical aspects of protein folding and stability - 5 ECTS

Application deadline

Registration deadline for PhD students at UiT - The Arctic University of Norway: February 1st Application deadline for external applicants: December 1st

Type of course

Theoretical and practical subject. The course is available as a singular or elective course independent of study program, also to exchange students and free-movers. The course is offered as a national course through the national PhD-school, BioStruct (http://biostruct.uit.no). The course is offered on condition that a minimum number of students register for the course. If the number of interested students exceeds the capacity of the course, 75% of the course admissions should be reserved students attending the PhD school, BioStruct.

Admission requirements

To take PhD courses you need to have at least a master's degree or equivalent.

In addition the following knowledge is recommended: basic knowledge in biochemistry, protein structure and thermodynamics.

PhD students at UiT The Arctic University of Norway register for the course through StudentWeb . Registrations for the spring semester starts December 1st, unless an earlier date is specified in the application deadline.

External applicants apply for admission through SøknadsWeb. Registrations for the spring semester starts October 1st.

All external applicants have to attach a confirmation of their status as a PhD student from their home institution.
Students who hold a Master of Science degree, but are not yet enrolled as a PhD-student have to attach a copy of their master's degree diploma. These students are also required to pay the semester fee.

More information regarding PhD courses at the Faculty of Science and Technology is found here.


Course content

The course will cover thermodynamic and kinetic aspects of protein stability and folding. Mechanisms and models for denaturation, folding and refolding of proteins will be discussed from both a thermodynamic and a kinetic angle of view. The thermodynamics of various states of the protein (native, unfolded and intermediate states) will be discussed, including the Molten globule state. Biophysical properties relevant to protein stability (hydrophobicity, charge, amino acid composition, solvent, secondary structure, etc) will be covered. Other topics will be folding kinetics, theoretical approaches for studying folding, and also a discussion of how to gain information about stability from amino acid sequences and from analyzing the 3D-structure of the native protein.
The course will additionally deal with issues like protein folding in connection with diseases and folding/refolding problems related to recombinant protein expression. Case studies on the use of ligands for stabilization of proteins will be covered, as well as on environmental adaptation of proteins related to stability (thermophiles, psychrophiles, halophiles, etc.).

-Methods for studying folding and stability will be covered: NMR, Calorimetry, Circular Dichroism (CD), and other spectroscopic techniques.

-Practical exercises using Differential Scanning Calorimetry (DSC) will be used to illustrate some of the concepts.


Objectives of the course

The candidate..

Knowledge

  • Has profound  knowledge about the main intramolecular forces involved in the stabilization of proteins; their origin, magnitude and roles in proteins.
  • Has extensive knowledge of the enthalpy and entropy contributions to the folding and unfolding processes of proteins.
  • Has in-depth knowledge about the temperature dependency of the solvation and desolvation of polar and non-polar groups in proteins.
  • Have basic knowledge about computer simulation techniques and how such methods can be utilised to study protein stability and protein folding and unfolding processes.
  • Has profound insight into the kinetics of protein folding processes.
  • Knows the characteristics of molten globule states.
  • Has knowledge about how various buffers can affect protein stability.
  • Has knowledge about mechanisms for chaperon aided protein folding.

Skills

  • Can describe forces involved in stabilizing the folded protein.
  • Can outline the influence of hydration on protein stability and folding, both for polar and non-polar groups the combined effect.
  • Is able to describe the mechanisms and kinetics of protein folding in general terms.

 

General competence

  • Understands the complexity of factors influencing protein stability and can suggest methods to study protein stability and folding.
  • Has the ability to read and understand in general terms, research papers where the protein stability and folding/unfolding are discussed. 


Language of instruction and examination

The language of instruction is English and all of the syllabus material is in English. Examination questions will be given in English, and may be answered either in English or Norwegian/Scandinavian language.

Teaching methods

The course is given intensively over two weeks.

Assessment

Oral exam approximately 2 weeks after the end of the course. Pass/fail evaluation. Mandatory participation to at least 80% of the activities.

Recommended reading/syllabus

The syllabus is defined by the lecture notes and material handed out during the course.

Error rendering component

  • About the course
  • Campus: Tromsø |
  • ECTS: 5
  • Course code: KJE-8701
  • Tidligere år og semester for dette emnet