Main Field of Study and progress level:
Chemistry: Second cycle, in-depth level of the course cannot be classified
Grading scale: Pass with distinction, Pass, Fail
Responsible department: Department of Chemistry
Established by: Faculty Board of Science and Technology, 2022-10-26
Revised by: Faculty Board of Science and Technology, 2023-09-15
Contents
Proteins are biological macromolecules that are essential for life. They perform key functions, such as providing structure to cells and tissues, catalyzing metabolic reactions, transporting molecules, or transmitting signals. These functions are determined by their chemical properties and physical interactions. This course covers the thermodynamic principles that lead to the structure, stability and interactions of proteins, and the theoretical basis of methodologies to study protein structure and function. The course provides hands-on experience with designing and performing experiments to investigate biophysical properties of proteins, and discussion on how these affect function. The course also covers computational tools to visualize the structure of proteins.
Expected learning outcomes
After completing the course, students shall be able to:
Identify different motifs and domains in protein structures and how these relate to function.
Understand and use the thermodynamic principles that determine the structure and folding of proteins, how and these impact function.
Understand and describe the methodologies to determine protein structure, and suggest which one is more adequate to study a particular protein.
Use the principles of molecular recognition to understand interactions with proteins.
Relate the theoretical framework of catalysis to its application to study enzyme function.
Use computational tools to visualize protein structure and to predict their function.
Design and perform experiments to study which aspects of the structure are important for the stability, structure, and function of proteins.
Critically discuss the results of experiments designed to study protein stability, structure, and function.
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 6/A.
Form of instruction
The course will take the form of lectures, group exercises, demonstrations, and laboratory experiments. Participation in the laboratory moments is mandatory.
Examination modes
The course will be examined through a written exam on the theoretical part, and written report and its verbal presentation and discussion on the laboratory part. The written exam is graded with Fail (U), Pass (G) or Pass with distinction (VG), and the laboratory part is graded with Fail (U) or Pass (G). 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 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 failed a course or part of a course twice is entitled to request appointment of another examiner, unless there are special reasons against it (HF Chap. 6 § 22). Requests for a new examiner should 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).
Literature
Valid from:
2023 week 40
The molecules of life : physical and chemical principles Kuriyan John., Konforti Boyana., Wemmer David. New York : Garland Science : 2013. : xxii, 1008 p. : ISBN: 978-0-8153-4188-8 Mandatory Search the University Library catalogue