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| Detailed information |
| Original study plan |
Master's programme Joint Master Programme Biological Chemistry 2010W |
| Objectives |
(*)Chemistry of peptides and proteins. Physical and chemical methods applied to the studies of protein structure. Protein structures in relation to their function. Structure of proteins.
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| Subject |
(*)Review the chemistry of peptides and proteins: Polymer of amino acid, the backbone of a polymer; Three-dimensional structure: Secondary structure, Fibrous proteins, Globular proteins, Protein stability, Quaternary structure; Protein folding and dynamics: Protein folding, theory and experiment, protein denaturation, folding pathway and prediction of protein structure; Protein dynamics; atomic fluctuations, collective motions and triggered, conformational changes; Experimental methods applied to study protein structures: Transport in electric field, Scattering by larger particles (X-rays diffraction by fibrous proteins, NMR, Circular dichroism, Laser raman, Neutron diffraction; Theoretical methods applied to study protein structures: homolgy modeling, molecular dynamics, ligand/docking, coarse graining; Allosteric regulation; Adair equation, Symmetry model, Sequential model and cooperativity
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| Criteria for evaluation |
(*)Oral examination
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| Methods |
(*)Lecture
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| Language |
English |
| Changing subject? |
No |
| Further information |
(*)Student Learning Goals. Students will:
• Have detailed insight into the structure of proteins with respect to protein chemical and biophysical experiments
• Have insight into the use of prediction methods and molecular modeling techniques
• Have knowledge and insight into protein folding in vitro and comparison to in vivo protein folding
• Have knowledge and insight into the general principles of protein purification (based on size, charge, hydrophobicity or on biospecific properties)
• Have knowledge of possible chemical modification reactions
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