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Molecular understanding of protein misfolding and aggregation in Parkinson’s disease
Each project will focus around biophysical studies of protein amyloid formation as a function of internal and external parameters using the key protein in Parkinson’s disease (alpha-synuclein) as primary target.
Proteins are linear chains of amino acids that must fold into unique 3D structures in order to function. Problems with protein folding underlie many human diseases. In amyloid diseases, such as Alzheimer´s, Parkinson's, type-2 diabetes, protein misfolding followed by assembly into long thin fibers result in toxicity. To find ways to cure these diseases, the molecular mechanisms of protein misfolding and aggregation, and how cellular factors affect these processes, must be identified. In our research, we use a range of standard and unique biophysical, spectroscopic, and biochemical techniques in combination with purified proteins and strategically mutated variants to address molecular-mechanistic questions. In each project, the student will learn how to make proteins and how to apply biophysical/biochemical methods; each student will work with a senior scientist in the group.
Proteins are linear chains of amino acids that must fold into unique 3D structures in order to function. Problems with protein folding underlie many human diseases. In amyloid diseases, such as Alzheimer´s, Parkinson's, type-2 diabetes, protein misfolding followed by assembly into long thin fibers result in toxicity. To find ways to cure these diseases, the molecular mechanisms of protein misfolding and aggregation, and how cellular factors affect these processes, must be identified. In our research, we use a range of standard and unique biophysical, spectroscopic, and biochemical techniques in combination with purified proteins and strategically mutated variants to address molecular-mechanistic questions. In each project, the student will learn how to make proteins and how to apply biophysical/biochemical methods; each student will work with a senior scientist in the group.
One goal is to obtain technical/laboratory skills by learning to express/purify proteins (E. coli expression, biochemical procedures, chromatography with ÄKTA) and how to use various biophysical equipment (e.g., circular dichroism, linear dichroism, calorimetry, fluorescence, light scattering, atomic force microscopy, and electron microscopy) along with data interpretation. The specific research question to be addressed in each project is to elucidate the effects on alpha-synuclein conformation and aggregation by (1) lipid vesicles of varying composition and size, (2) metals/metal-binding proteins, (3) DNA/RNA interactions, or (4) chaperone proteins, all as a function of disease-causing point mutations in alpha-synuclein. You can choose between directions 1 to 4, or projects can be tailored-made to suit students’ interests or particular skills.
One goal is to obtain technical/laboratory skills by learning to express/purify proteins (E. coli expression, biochemical procedures, chromatography with ÄKTA) and how to use various biophysical equipment (e.g., circular dichroism, linear dichroism, calorimetry, fluorescence, light scattering, atomic force microscopy, and electron microscopy) along with data interpretation. The specific research question to be addressed in each project is to elucidate the effects on alpha-synuclein conformation and aggregation by (1) lipid vesicles of varying composition and size, (2) metals/metal-binding proteins, (3) DNA/RNA interactions, or (4) chaperone proteins, all as a function of disease-causing point mutations in alpha-synuclein. You can choose between directions 1 to 4, or projects can be tailored-made to suit students’ interests or particular skills.
This project is available to students of the http://idealeague.org partner universities. If this research topic sounds interesting and you have some background knowledge in biochemistry, molecular biology, and biophysical chemistry, please contact us and you will get more information. Students can apply any time during the year as we have no particular start date. Welcome!
Duration: one or two semesters (30 or 60 Credits)
University: Chalmers University of Technology, Gothenburg, Sweden
Department/Division: Biology and Biological Engineering/ Chemical Biology
Contact: Professor Pernilla Wittung Stafshede (pernilla.wittung@chalmers.se)
This project is available to students of the http://idealeague.org partner universities. If this research topic sounds interesting and you have some background knowledge in biochemistry, molecular biology, and biophysical chemistry, please contact us and you will get more information. Students can apply any time during the year as we have no particular start date. Welcome!
Duration: one or two semesters (30 or 60 Credits)
University: Chalmers University of Technology, Gothenburg, Sweden
Department/Division: Biology and Biological Engineering/ Chemical Biology
Contact: Professor Pernilla Wittung Stafshede (pernilla.wittung@chalmers.se)
Each year the IDEA League offers the students of its partner universities over 180 monthly grants for a short-term research exchange. In general, these grants are awarded based on academic merit. For more information visit http://idealeague.org/student-grant/