Lecturer(s)
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Course content
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Chemistry of peptides and proteins. Physical and Chemical methods applied to the studies of protein structure. Protein Structures in relation to their function. Contents: Chemistry of peptides and proteins: Polymer of amino acid; Threedimensional structure: Secondary structure, Fibrous proteins, Globular proteins, Protein stability, Quaternary structure; Protein folding and dynamics: Protein folding, 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, interaction of EM radiation with particles (X-rays diffraction by fibrous proteins, NMR, Circular dichroism, Laser raman, Neutron diffraction; Theoretical methods applied to study protein structures: homology modeling, molecular dynamics, ligand/docking; Allosteric regulation;
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Learning activities and teaching methods
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Monologic (reading, lecture, briefing), Dialogic (discussion, interview, brainstorming)
- Preparation for classes
- 25 hours per semester
- Class attendance
- 39 hours per semester
- Preparation for exam
- 25 hours per semester
- Preparation for credit
- 10 hours per semester
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Learning outcomes
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Chemistry of peptides and proteins. Physical and Chemical methods applied to the studies of protein structure. Protein Structures in relation to their function. Contents: Chemistry of peptides and proteins: Polymer of amino acid; Threedimensional structure: Secondary structure, Fibrous proteins, Globular proteins, Protein stability, Quaternary structure; Protein folding and dynamics: Protein folding, 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, interaction of EM radiation with particles (X-rays diffraction by fibrous proteins, NMR, Circular dichroism, Laser raman, Neutron diffraction; Theoretical methods applied to study protein structures: homology modeling, molecular dynamics, ligand/docking; Allosteric regulation;
Final Competences - to have detailed insight in the structure of proteins with respect to protein chemical and biophysical properties - to have insight in the use of prediction methods and molecular modeling techniques - to have knowledge of and to have insight in protein folding in vitro and comparison to in vivo protein folding - to have knowledge of and to have insight in the general principles of protein purification (based on size, charge, hydrophobicity or on biospecific properties) - to have knowledge of possible chemical modification reactions
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Prerequisites
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knowledge from courses: Biochemistry 1, Biochemistry 2, Biochemistry Laboratory 1, Biochemistry Laboratory 2, Biomolecular NMR Spectroscopy
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Assessment methods and criteria
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Oral examination, Student performance assessment
The student must pass the practical part, participate on lectures and actively discuss the topics. The students must understand the following topics to successfully pass the exam: protein folding, protein purification techniques, protein structure modelling techniques etc.
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Recommended literature
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Lesk, Arthur M. Introduction to protein science: architecture, function, and genomics / Arthur M. Lesk. 1st ed. Oxford : Oxford University Press, 2004. 310 s..
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Petsko, G & Ringe, D. Protein Structure and Function, New Science Press in association with Sinauer Associatesand Blackwell Science, London. 2003. 180 pp..
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