Protein Research Lab - Intrinsically Disordered Proteins
Course content
This is a research-integrating experimental laboratory course. It is based on a seven weeks teaching period with 3 x 8 hours/week of student directed research on intrinsically disordered proteins (IDPs) including protein expression and purification, followed by experimentally addressing a self-defined testable hypothesis through biophysical studies.
The course totals 80 hours of obligatory laboratory work and
introductory part on IDPs and 2 weeks of presentations (planning
and execution).
The two weeks at the end of the course are reserved for oral
presentations of scientific data through an oral session presenting
purification strategy and results, followed by a scientific
poster session, where the obtained data are presented in front of a
poster committee and the potential collaborative partner.
Here suggestions for further research are
presented.
Experimental part
The course focuses exclusively on intrinsically disordered proteins
(IDPs), and integrates ongoing IDP research with teaching. It
follows the concept of student-directed
research and includes the Beyond The
Books and IDP4Real
initiatives. The student can choose
between different IDPs, either with an academic interest and
collaborator, or with an industrial partner, and will define a
project based on a hypothesis, that includes recombinant expression
of the chosen proteins, design of purification strategies,
purification and characterization. Methods include fractionation
methods, electrophoresis, chromatography (size exclusion, affinity,
heparin columns, ion exchange, reversed phase, protease-driven
tag-release etc.), peptide mass finger printing, applied
bioinformatics, chemical modification, and mass spectrometry. It
also includes CD-, fluorescence-, and NMR-spectroscopy, isothermal
titration calorimetry, small-angle X-ray scattering, molecular
graphics and modelling, ligand binding and dataprocessing and
presentation. The laboratory course of 80 hours is distributed over
seven weeks and students work in research teams of 3-4 student
researchers. An inspirational lecture from an international
expert in the IDP field as well as an introduction to ensemble
modeling of IDPs are included, allowing visualization of the
ensemble of the chosen IDP. Given the nature of
research-integrating teaching, risk assessment and data-based
experimental re-design are included aspects. All proteins have
never been expressed and studied before at UCPH.
At the end of the laboratory course, each group presents its data by an oral presentation with discussion and at a scientific poster session of 2 hours where they present their own poster, which will include suggestions for further research. A scientific board consisting of external evaluators will discuss the poster.
MSc Programme in Biochemistry
Knowledge:
- Understand and describe IDPs in terms of biophysical properties and functional advantages
- Describe and understand details of the chemical and physical properties of IDPs, and how this can be exploited for their isolation and how this related to function
- Describe how NMR, SAXS and CD can be used to characterize IDPs
- Explain mechanism of folding-upon-binding, and describe and apply methods for studies of IDPs
- Describe physical forces in terms of energy, range and dependence on geometry, environments and other parameters of importance
- Describe and understand the principle of SDS-PAGE including the stacking effect
- Describe and understand basic chromatographic theory
- Describe thermodynamically the underlying physical chemistry in protein interactions and calculate thermodynamic parameters from selected data presented in graphics
Skills:
- Evaluate the relative advantages and disadvantages of NMR, CD, and SAXS approaches for IDP analysis
- Demonstrate a thorough understanding of a selection of modern protein biophysical, spectroscopic and chemical experimental and analytical methods and assessment of when to use which method for solving a specific problem
- Understand and evaluate thermodynamics of protein folding and interactions involving IDPs
- Describe and evaluate methods for protein quantification
- Design purification procedures based on predefined protein properties
- Evaluate and conclude on protein purity from appropriate methods
- Analyze experimental data from protein purification protocols
- Quantitatively analyze and evaluate IDP interactions
- Describe and understand the use of methods applied in IDP interactions including CD, ITC, fluorescence, SAXS and NMR spectroscopy
- Evaluate methods and theoretical approaches to address questions in relation to research on IDPs
- Execute protein purification and characterization experiments
- Define testable hypotheses in relation to experimental protein science involving IDPs
- Perform an ensemble modeling of an IDP using computational tools.
- Integrate experimental data to reweight computationally generated proteins ensembles
- Use different digital tools to fit, model and present the data and evaluate the appropriateness of the model(s)
- Use graphical digital tools to produce figures that present scientific data in a communicative way.
Competences:
- Critically evaluate experimental results from studies of protein primary and secondary structure using protein chemistry
- Differentiate between physical forces in terms of energy, range and dependence on geometry, environments and other parameters of importance
- Critically evaluate advantages and disadvantages of different procedures used for purification and characterization of IDPs
- Cite, evaluate and understand various heterologous protein expression systems including various tags
- Critically evaluate experimental biophysical results
- Critically evaluate experimental data on ensembles
- Analyze, evaluate and condense experimental data in protein science from combinations of all possible areas of the curriculum to solve relevant research questions in relation to IDPs
- Demonstrate written- and oral communication in a protein scientific language
- Define, attack and present a scientific problem regarding IDPs (oral and poster presentation)
- Communicate verbally in a scientific language and present published scientific results in power points in a clear and informative way
- Design strategies to test scientific hypotheses experimentally
- Design, execute, critically evaluate, and present experiments in protein chemistry
- Design a scientific poster of personally generated scientific data and present this in front of an audience
An 80 hours obligatory lab-course disseminated over 7 weeks. A total of 14 hours of obligatory oral presentations and scientific discussions.
See Absalon
It is recommended that the student has passed a basic course in
protein science such as Protein Videnskab og Enzymology (PVEt)
(Biochemistry), Protein structure and function (Chemistry), Protein
Chemistry and Enzymology I and II (Molecular Biomedicine), Protein
Chemistry and Enzymology for Biologists (Biology) or Bio-structural
chemistry (Pharmaceutical sciences).
As the course require some knowledge on protein chemistry, we do
not recommend that the student has passed only a basic biochemistry
course. A prior course in protein science/biophysics/physical
chemistry is highly recommended.
Students who have passed all first-year courses and half of the
second year courses (corresponding to a total of 90 ECTS) of their
curriculum would have obtained competencies that would enable them
to follow the course, including the recommendations for basic
courses listed above.
Academic qualifications equivalent to a BSc degree is
recommended.
If you have passed or followed Protein Science A, you are still eligible for attending this course.
Oral feedback both individually and in groups on oral presentations and written presentations in the form of a scientific poster presenting the results of the laboratory work.
- ECTS
- 7,5 ECTS
- Type of assessment
-
Continuous assessment
- Type of assessment details
- 80% attendance in laboratory exercises.
An oral presentation of results in a powerpoint and a written presentation in the form of a poster is required. The poster must also be orally presented in front of an academic or industrial partner and in front of a poster committee. - Aid
- All aids allowed
- Marking scale
- passed/not passed
- Censorship form
- No external censorship
Several internal examiners.
- Re-exam
-
The same as the ordinary exam, but the oral presentations will be individuel and presented in front of the lecturers
If the attendance in the laboratory exercises is less than 80% the student has to take the course again next year.
Criteria for exam assessment
See Learning Outcome.
Single subject courses (day)
- Category
- Hours
- Lectures
- 10
- Preparation
- 80
- Practical exercises
- 80
- Project work
- 36
- Exam
- 0
- English
- 206
Kursusinformation
- Language
- English
- Course number
- NBIK22003U
- ECTS
- 7,5 ECTS
- Programme level
- Full Degree Master
- Duration
-
1 block
- Placement
- Block 1
- Schedulegroup
-
B And C
- Capacity
- 32
The number of places might be reduced if you register in the late-registration period (BSc and MSc) or as a credit or single subject student. - Studyboard
- Study Board for the Biological Area
Contracting department
- Department of Biology
Contracting faculty
- Faculty of Science
Course Coordinator
- Birthe Brandt Kragelund (3-71717a4f71787e3d7a843d737a)
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