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Experimental Structural Biology, 7,5 credits

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The course syllabus was confirmed by the Faculty board for graduate studies 4 April 2017. The course is at the PhD level and amounts to 7.5 credits.
The course syllabus is formally approved in Swedish. This is a translation.

Learning outcomes

The course aims to provide a deeper understanding of some of the most important experimental methods used to determine the three-dimensional structures of proteins, as a basis for understanding their biological functions. We also aim at an understanding of the forces that underpin the three-dimensional structure of proteins, as well as a basic understanding of the methods used in structure-based drug design.

On completion of the course, participants shall be able to:

• demonstrate good understanding of the three-dimensional structure of proteins, their stability, interactions and dynamics
• explain the theoretical basis for X-ray crystallography
• Perform X-ray crystallograpy experiments at a basic level, from which the participant can further develop the skills on his/her own.
• demonstrate basic knowledge of how nuclear magnetic resonance (NMR), neutron diffraction and small-angle X-ray and neutron scattering can be used to produce specific information in addition to X-ray crystallography
• assimilate and critically evaluate the scientific literature dealing with protein structure and function, particularly in terms of the experimental methods.
• demonstrate basic knowledge on how structural information can be used in the development of modern pharmaceuticals

Course content

Lectures:
Basic knowledge of protein structure: polypeptide conformation. Protein secondary and three- dimensional structure. Stability, dynamics and interactions of proteins: packing and electrostatics. Principles of X-ray crystallography, neutron crystallography, small angle X-ray and neutron scattering. Ligand binding and structure-based drug design.
Laboratory work and computer exercises:
Training in the relevant theoretical and experimental methods described for the study of protein structure and dynamics. Includes protein crystallization, data collection at MAX IV, data processing, structure determination and modelling, as well as a simple exercise in ligand docking.

Teaching forms

Teaching consists of lectures, computer exercises, demonstrations, study visits to Lund Protein Production Platform (LP3) and MAX IV, and laboratory work. All instruction except lectures
are mandatory. The course consists of ca. 5 weeks of teaching from the Masters level course KEMM15/KEMM35 (15 hp).

Assessment

The assessment is based on a report on laboratory and computer exercises, on a written exam, and on mandatory items. Students who fail in the examination are offered another test shortly afterwards.

Grading scale

Possible grades are Pass and Fail. To pass the course, the written report must be approved, the written exam must be passed, and all mandatory items must be completed.

Language of instruction

The course is given in English.

Entry requirements

Admitted to third cycle studies in a relevant subject.

Additional information

Literature according to a list that will be available on the Chemistry department's website at least five weeks before the start of the course. The course is given also in the second cycle, under the course code KEMM15/KEMM35. Students who have been awarded credits for KEMM15/KEMM35 cannot also get credits for the corresponding parts of NAKE011, and vice versa.

Course responsible teacher and unit/division

Derek Logan
Email: derek.logan@biochemistry.lu.se

Center for Molecular Protein Science (CMPS) , KILU

Do you have questions? Please contact viveka.alfredsson@chem.lu.se