Biochemistry: Protein Structure and Function, 15 Credits

Contents

Protein Structure and Function is a central theme in a large part of modern research and biotechnological operations. In order to be able to understand biological and biochemical processes at a molecular level, it is often necessary to know the structure of a specific protein. The course aims, primarily, to provide in-depth knowledge of protein structures, as well as how they are constructed, how they work and how they are stabilised. Proteins will be studied both from a theoretical and a practical, laboratory perspective. This encompasses the proteins' evolution, structure, dynamics, thermodynamics, stability and folding. The course also comprises studies of specific proteins and their domains, including membrane proteins, antibodies, enzymes and DNA-binding proteins. Proteins are easiest to visualise using molecular graphics, and part of the course is devoted to studying the structure and function of proteins with the help of molecular graphics programmes. The  laboratory-based part of the course provides practical skills in studying the proteins' stability and folding, using modern biophysical instruments. Emphasis is also placed on the construction of models, in order to interpret and analyse the raw data collected. A literature seminar is held where the starting point is a relevant academic article.

Expected learning outcomes

After completing the course, students shall be able to:

• discuss the evolution of proteins
• describe how proteins are constructed
• describe the interactions that hold proteins together
• describe how a protein is stabilised thermodynamically
• describe how protein structures can be determined
• describe and discuss the most important domain structures of proteins
• describe and discuss the relationship between the structure and function of proteins and how targeted mutagenesis is used to acquire knowledge about such relationships
• use molecular graphics to analyse and visualise protein structures
• conduct computerised literature searches
• present academic dissertations in seminar format.
• design and conduct experiments in order to study the folding and stability of proteins
• present an academic piece of work in dissertation format

Required Knowledge

90 ECTS credits including the course Biochemistry 15 ECTS credits (5KE020/075) or Biochemistry, Protein Chemistry and Enzyme Kinetics 15 ECTS credits (5KE076) or equivalent and English B/6.

Form of instruction

The teaching may take the form of lectures, lessons, group exercises, demonstrations and laboratory experiments. The laboratory experiments and computer assisted exercises mandatory.

Examination modes

Examination is conducted partly through written examinations (on the theoretical section), and partly through written and verbal accounts of the laboratory elements as well as participation in molecular graphics exercises. For written examinations, as for the laboratory element, the grades Fail (U), Pass (G) or Pass with distinction (VG) are awarded. For the whole course, the grades Fail (U), Pass (G) or Pass with distinction (VG) are awarded. To pass the whole course, all examinations and obligatory elements must have been passed. The grade constitutes an overall assessment of the results of the various different parts of the examination and is not allocated until all mandatory elements are complete. Those who pass an examination may not take the same examination again with the aim of achieving a higher grade. A student who has taken two examinations for a course or a part of a course, without passing either examination, has the right to have another examiner appointed, if there are no specific reasons for not doing so (Chapter 6, Section 22, HEA). Requests for a different examiner are to be made to the Head of the Department of Chemistry.

For students who have not been approved at the regular exam, a new exam is arranged in accordance with Umeå University's Rules for grades and examination (FS 1.1-574-22). The first re-exam is offered no later than two months after the regular exam. With the exception of cases where the regular exam takes place in May or June, a first re-examination is offered instead within three months of the regular exam. In addition, at least one further re-examination is offered within one year from the regular exam date.

Examiners may decide to deviate from the modes of assessment in the course syllabus. Individual adaption of modes of assessment must give due consideration to the student's needs. The adaption of modes of assessment must remain within the framework of the intended learning outcomes in the course syllabus. Students who require an adapted examination must submit a request to the department holding the course no later than 10 days before the examination. The examiner decides on the adaption of the examination, after which the student will be notified.
 

Other regulations

In the event that the syllabus ceases to apply or undergoes major changes, students are guaranteed at least three examinations (including the regular examination opportunity) according to the regulations in the syllabus that the student was originally registered on for a period of a maximum of two years from the time that the previous syllabus ceased to apply or that the course ended.

ACCREDITATION Accreditation requests are always examined individually (see the University's Rules and Regulations and the Accreditation Regulations).