Structure and Dynamics of Biomolecules

The course is classified at the level 90-120 credits for Degree of Bachelor and can be counted as a course at second cycle level for Degree of Master (120 credits). The course can be read as a freestanding course. The course can be read as free-standing course.

The course can be part of the following programmes: 1) Molecular Biology, Master's Programme (N2MBI), 2) Chemistry and learning, Master's Programme (N2KOL), 3) Master's Programme in Organic and Medicinal Chemistry (N2KEL), 4) Master's Programme in Chemistry (N2KEM), 5) Bachelor of Science Programme in Medicinal Chemistry (N1LMK), 6) Bachelor of Science Programme in Chemistry (N1KEM) and 7) Biology, Master's Programme (N2BIO)

The admission requirements are 120 credits within Science, 45 credits of these should be in Chemistry, including KEM060, Biochemistry, 15 credits or equivalent education.

Applicants must prove their knowledge of English: English 6/English level 2 from Swedish Upper Secondary School or the equivalent level of an internationally recognized test, for example TOEFL, IELTS.

The course consists of a lecture block on the theory of X-ray crystallography, NMR spectroscopy and Electron Microscopy, which are the major method in structural biology of macromolecules. This is complemented by laboratory exercise in X-ray crystallography, NMR spectroscopy and Electron Microscopy. The third part of the course is a critical analysis of relevant scientific literature using flipped classrooms. The students communicate via written abstracts and give lectures, which is complimented by introductory lectures into the scientific literature to be examined by the teachers.

The emphasis of the course is on experimental methods and can be divided into three parallel sub-courses:

1. Methods of structural biology (7.5 credits)

The sub-course provides advanced knowledge of biomolecules with regard to:

• structure
• function

as well as about the following experimental methods:

• crystallisation
• X-ray diffraction and scattering techniques
• nuclear magnetic resonance (NMR) spectroscopy
• electron microscopy (EM)

2. Practical structure analysis of biomolecules (**3 credits)**

The sub-course provides advanced practical knowledge of structural analysis with X-ray diffraction techniques, nuclear magnetic resonance spectroscopy (NMR) and electron microscopy.

3. Applied stuctural biology (4.5 credits)

The sub-course provides in-depth knowledge of the structure of biomolecules in cells:

• cytoskeleton
• ion channels
• receptor mechanism of action
• other proteins with significance in neuroscience

and additional methods such as:

• machine learning and structural prediction (ML)
• structure based drug design (SBDD)

Knowledge and understanding

After completing the course the student should be able to:

Sub-course 1:

• account for the structure of biomolecules on an advanced level
• account for modern biophysics and biomolecular structural research methods and be ready for further research studies on the subject
• account for the concepts of structure-based drug design

Sub-course 2:

• account for practical knowledge of methods for characterisation of proteins and determination of their three dimensional structure
• account for different analytical tools such as molecular graphics and Fourier transformation.

Sub-course 3:

• account for several examples where structural biology has had impact on the understanding of cells
• account for the concepts of structure-based drug design

Competence and skills

After completing the course the student should be able to:
Sub-course 2:

• account for practical knowledge of methods for determination of three-dimensional structure in biomolecules
• implement basic experimental tasks as protein crystallization
• interpret, discuss and present laboratory results as well as draw reasonable conclusions

Sub-course 3:

• independently and creatively analyse structure and function of a protein
• identify and use relevant research literature
• clearly present and discuss, orally as well as in writing, their conclusions and the knowledge and the arguments they are based upon, in dialogue with different groups, in both national and international contexts

Judgement and approach

After completing the course the student should be able to:

Sub-course 1:

• critically assess theoretical possibilities and limitations of various experimental methods

Sub-course 2:

• critically assess the practical possibilities and limitations of different experimental methods.

Sub-course 3:

• critically assess the possibilities and limitations of various experimental methods in the literature.

Sub-course 1: The instruction is given in the form of lectures.

Sub-course 2: The instruction includes laboratory sessions and presentations.

Sub-course 3: The instruction in the form of lectures and individual assignments including a presentation in the form of flipped classroom.

Sub-course 1: Examination takes place through written examinations. For students who have not passed the regular examination additional examination sessions are offered.

Sub-course 2: Assessment is based on laboratory sessions and presentations.

Sub-course 3: Assessment is done through a written and oral presentation of assignments.

If a student who has been failed twice for the same examination element wishes to change examiner before the next examination session, such a request is to be granted unless there are specific reasons to the contrary (Chapter 6 Section 22 HF).

If a student has received a certificate of disability study support from the University of Gothenburg with a recommendation of adapted examination and/or adapted forms of assessment, an examiner may decide, if this is consistent with the course’s intended learning outcomes and provided that no unreasonable resources would be needed, to grant the student adapted examination and/or adapted forms of assessment.

If a course has been discontinued or undergone major changes, the student must be offered at least two examination sessions in addition to ordinary examination sessions. These sessions are to be spread over a period of at least one year but no more than two years after the course has been discontinued/changed.

If a student has been notified that they fulfil the requirements for being a student at Riksidrottsuniversitetet (RIU student), to combine elite sports activities with studies, the examiner is entitled to decide on adaptation of examinations if this is done in accordance with the Local rules regarding RIU students at the University of Gothenburg.

The grading scale comprises: Pass with Distinction (VG), Pass (G) and Fail (U).

Sub-course 1: The grading scale comprises: Pass with Distinction (VG), Pass (G) and Fail (U). The grade corresponds to the result from the written examination.

Sub-course 2: The grading scale comprises: Pass (G) and Fail (U). To pass are required participation in all laboratory sessions and approved laboratory reports.

Sub-course 3: The grading scale comprises: Pass with Distinction (VG), Pass (G) and Fail (U). Grade is decided by project work and presentation.

Final grade: For grade Pass (G), at least grade Pass (G) in all sub-courses is required. For grade Pass with distinction (VG), in addition grades Pass with distinction (VG) on modules 1 and 3 are required.

Students who participate in or have completed course should be given possibility to anonymously perform experiences of and views in the course in a course evaluation.

The results of and possible changes to the course will be shared with students who participated in the evaluation and students who are starting the course.

Language of instruction: English

The course replaces course KEM450, Structural biochemistry, and the two courses may not be counted in together for a degree.