Protein Science A (ProtSciA)
Seven weeks teaching period with 4 x 2 hours theoretical
teaching a week and 80 hours of obligatory laboratory work
distributed over six weeks. Teaching will be in a colloquium
format with a total of 9-12 subjects covered. Each subject is
assigned either 2x2 hours or 1x2 hours. Each session will
consist of one or more of: lecturing, problem solving, student
seminars, concepts, case-based teaching, computer assignments, and
One week is reserved for oral presentations of scientific data in a seminar format.
The course consists of two parts:
- Theoretical part: this is very similar to the
course "Protein Science C". The theoretical part focuses
on the physics, chemistry, structure and function of proteins in
their biological environments. A generel part is complemented by a
more specific part. General subjects include: protein chemistry
methods and strategies, protein structures and structure
determination, folding and misfolding, proteome
analysis. Specific subjects include protein physics,
thermodynamics, protein-protein interactions, protein design and
engineering, protein dynamics, misfolding and disease.
- Experimental part (cannot be followed
separately): Follows the concept of student-directed
research. The student can choose between different
projects that includes recombinant expression of proteins and
engineered variants, design of purification strategies,
purification and characterisation. Methods include
fractionation methods, electrophoresis, chromatography (size
exclusion, affinity, ion exchange, reversed phase etc.), Western
blot (antibody based) analysis, pull-down and immune precipitation
assays, yeast-2-hybrid analysis, peptide mass finger printing,
protein crystallization, applied bioinformatics, chemical
modification, and mass spectrometry. It includes also CD-,
fluorescence-, and NMR-spectroscopy, isothermal titration
calorimetry, molecular graphics and modelling, ligand binding, pKa
determination and data processing and presentation. The
laboratory course of 80 hours is distributed over six weeks and
students work in research teams of 3-4 student
At the end of the laboratory course, each group present its data by an oral presentation and at a scientific poster session of 3 hours where they present their own poster. A scientific board consisting of lecturers on the course or of external evaluators evaluates the posters.
BSc Programme in Biochemistry
- Describe and understand details of the chemical and physical properties, reactivity and experimental analysis of amino acids, both in isolation and in the context of protein structures
- Explain and describe methods for the determination of protein structures
- Describe the basic methods and principles of NMR including its applications for protein characterization
- Describe and understand basic principles in small-angle X-ray scattering
- Explain the principles of cryo-electron microscopy and how it is applied in protein structure analysis
- Understand and describe intrinsically disordered proteins in terms of biophysical properties and functional advantages
- Explain mechanism of folding, and describe and apply methods for studies of protein folding and stability in vitro
- Describe and understand mechanisms for protein misfolding
- 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 and understand membrane protein structure
- Describe the concepts of hydropathy plots in relation to membrane protein structure
- Describe thermodynamically the underlying physical chemistry in protein interactions and calculate thermodynamic parameters from selected graphical presentations
- Describe and understand the following terms: protein sequence, homology, orthologous and paralogous proteins, domain swapping, protein annotation, distance matrix, phylogenetic tree
- Describe and understand concepts, strategies, and methods in proteomics and functional genomics
- Describe and understand basic concepts in protein engineering especially in relation to enzymes
- Describe selected methods for high-throughput protein science
- Participate in a seminar on latest topics in protein science
- Integrate amino acid properties and modifications in relation to chemistry, disease and enzyme design
- Explain the practical matters of small angle x-ray scattering in relation to protein structures
- Evaluate data from small angle x-ray scattering
- Evaluate Guinier, Kratky plots and distribution functions
- Evaluate the relative advantages and disadvantages of crystallographic, cryo-EM and NMR approaches for protein structure analysis
- Evaluate qualities of experimental protein structures
- 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 stability for two-state folders and understand protein folding intermediates
- Evaluate free energy landscapes and folding funnels
- Analyse phi-values in relation to transition states for protein folding
- Relate the effect of protein stability in disease
- Describe and evaluate methods for protein quantification
- Design purification procedures based on predefined protein properties
- Evaluate and conclude on protein purity from appropriate methods
- Analyse experimental data from protein purification protocols
- Quantitatively analyse and evaluate protein-ligand and protein-protein interactions
- Understand and differentiate between agonism, antagonism and inverse antagonism
- Evaluate principles of protein regulation, active site chemistry and binding
- Diagnose binding reactions qualitatively and quantitatively and analyse these
- Describe and understand the use of methods applied in protein-ligand interactions including ITC, surface plasmon resonance, fluorescence and NMR spectroscopy
- Cite and understand the use of methods applied in proteomics and functional genomics including mass spectrometry, SILAC, MS/MS, 2-D gel electrophoresis, protein and DNA arrays, fluorescence resonance energy transfer, yeast two-hybrid, pull-down assays
- Cite and understand the use of applied protein bioinformatics (BLAST homology searches)
- Describe simple protein structures
- Evaluate methods and theoretical approaches to address questions in relation to protein science
- Execute protein purification and characterization experiments
- Define testable hypotheses in relation to experimental protein science
- Describe and understand the concept of hydrogen exchange in proteins
- Critically evaluate experimental results from studies of protein primary and secondary structure using protein chemistry
- Integrate and evaluate protein structure-function relationships
- 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 proteins purification and characterization
- Cite, evaluate and understand various heterologous protein expression systems
- Demonstrate insight into membrane protein purification problems and procedures
- Demonstrate a thorough understanding of the structure/function relationship of various membrane protein families
- Integrate experimental and theoretical data in membrane protein structure analysis and integrate these in relation to pharmaceutical science
- Understand and differentiate between negative and positive cooperativity in binding
- Demonstrate insight into isotope labelling, sequential assignments and evaluate the quality of NMR spectra
- Critically evaluate experimental results from proteome analysis
- Critically evaluate experimental data on enzyme mechanisms, function, and control
- Analyze, evaluate and condense experimental data in protein science from combinations of all possible areas of curriculum to solve relevant protein science problems
- Demonstrate written- and oral communication in a protein scientific language
- Defining, attacking and presenting a scientific problem in protein chemistry (oral 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 the students own scientific results and present this in front of an audience
Colloquium teaching - a mixture of lecturing, problem solving, theory exercises, student seminars, practical exercises, computer assignments, scientific discussions and student presentations. Practical laboratory exercises with project work presented at a poster session.
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),
Nanobio1+2 (nanoscience), Protein Chemistry and Enzymology I and II
(Molecular Biomedicine) or General Biochemistry 2 - Protein
Chemistry and Enzymology for Biologists (Biology).
As the course require some knowledge on protein chemistry, it is not recommended that the student has only passed a basic biochemistry course.
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, most preferably including the recommendations for basic courses listed above.
A second team will be made only when a minimum of 48 students are signed up for the 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.
- 15 ECTS
- Type of assessment
Written examination, 2 hours under invigilationOral examination, 20 minutes
- Type of assessment details
- Oral examination initiated from a set of predefined questions
without preparation time.
One overall grade will be given with 50% weight on each exam.
Both the oral and the written part of the exam must be passed individually.
The course has been selected for ITX exam
See important information about ITX-exams at Study Information, menu point: Exams -> Exam types and rules -> Written on-site exams (ITX)
- Only certain aids allowed
Calculator and the PC system "Maple".
As the exam is an ITX-exam, the University will make computers available to students at the exam. Students are therefore not permitted to bring their own computers, tablets, or mobile phones.
- Marking scale
- 7-point grading scale
- Censorship form
- No external censorship
Criteria for exam assessment
In order to obtain the grade 12 the student should convincingly
and accurately demonstrate the knowledge, skills and competencies
described under "Learning Outcome".
The student should also:
- Have participated actively in the laboratory course.
- Provide a critical and detailed oral and poster presentation of the practical part of the lab course.
- Give an oral presentation regarding experimental data from a primary paper.
- Have participated actively in the oral- and poster presentations from the lab course and in the oral science presentations.
Single subject courses (day)
- Class Instruction
- Practical exercises
- Project work
- Course number
- 15 ECTS
- Programme level
- Block 1
Outside timetable structure. Experimental course where all schedule
groups can be used.
The number of seats may be reduced in the late registration period
- Study Board for the Biological Area
- Department of Biology
- Faculty of Science
- Birthe Brandt Kragelund (3-65656e43656c72316e7831676e)
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Courseinformation of students