Spring. This course has a limited capacity, enrolment is based on application. Application deadline is Thursday in week 2 for the spring semester.
Please see this page for more information: https://www.uib.no/en/matnat/53431/admission-courses-limited-capacity
You will receive confirmation of whether you received a spot in Studentweb no later than Tuesday the week after the deadline.
The first lecture/orientation meeting is compulsory, which means you will lose your spot if you do not attend class that day. The time of the first lecture/orientation meeting can be found in the schedule on the course website or on the "Mitt UiB" learning platform.
Objectives and Content
The course aims to give students knowledge about the relationship between biomacromolecules structure and their function. There will be an emphasize on how several biomacromolecules assembles into functional assemblies and how these give rise to cellular function.
Proteins will get the main focus of this course. Topics that will be covered include how amino acids are assembled into primary, secondary, tertiary and higher order structures and complexes, and how functional protein properties then emerge. How these physical, biochemical and biological properties are utilized in living organisms will then be discussed. Other biomolecules and assemblies of biomolecule will generally only be discussed in connection with their relationship to proteins. The course will build on concepts that has already been introduced earlier, including protein folding, allostery, catalysis and enzymology, ligand and effector binding, post-translational modifications, and signaling. An important aspect of the course will be how all these phenomena regulates, and is regulated by, protein function. The course will offer introductions into relevant methodology, in particular how one determine protein structures experimentally. The course will also discuss protein evolution from a structural perspective.
On completion of the course the student should have the following learning outcomes defined in terms of knowledge, skills and general competence:
The student can explain in detail about
- the different levels og protein structure, from the amino-acid level to larger, quaternary complexes
- How proteins are synthetized, folded, and modified, and how these processes affect their function
- forces and effects that leads to the formation of protein structures
- how a protein uses its structural organization to achieve traits that do not occur in its individual components
- how these properties underpin function at the molecular level in a living organism
- how these protein functions are controlled by modification, localization and effector interactions
- relevant methodology to study biomacromolecules in vitro and in vivo
The student is able to
- explain (orally and in writing) how the topics outlined above acts together in cell processes such as signal transduction, endo / exocytosis, cell motility and gene regulation
- choose the right methodology in order to answer simple (and possibly also difficult) questions linked to a given macropmolecualr problem
- orient themselves in the spatial- and temporal scale that is associated with macromolecalar understanding
- solve math- and theoretical tasks related to the topics discussed in the course
- use Pymol, a program for working with protein structures, at a novice level.
- work in a group to produce a (compulsory) written assignment about a MOL310 relevant topic of the group¿s choice. The assignment must hold a good level with respect to student insight, clarity of presentation and proper use of terminology.
The student has
- the ability to place concepts discussed in MOL310 into a wider biological and chemical context, and moreover, reach their own conclusions independently of exisiting material
- understood how particular protein achieves its specific and unique characteristics
- the ability to convey qualitative and quantitative aspects of structural molecular biology, by oral and written means, to both specialists and non-specialists
- the ability to navigate to and understand content in The Protein Databank.
Required Previous Knowledge
Bachelor's degree in molecular biology, or equivalent background.
Compulsory Assignments and Attendance
Mandatory attendance to orientation meeting about written assignments.
Obligatory activities are valid for total six semesters.
The first lecture/orientation meeting is compulsory.
Forms of Assessment
Written assignment (25 %) and written exam (4 hours). Written exam counts 75 % and the written assignment 25 % of final grade. The written exam and the written assignment must be completed and compulsory activity approved, to obtain a grade in the teaching semester.
For a semester without teaching, the student may take the final exam if written assignment is approved. The result of the exam will constitute 75%, and the written assignment 25 % of final grade.
Examination support materials: Non- programmable calculator, according to model listed in faculty regulations
The grading scale used is A to F. Grade A is the highest passing grade in the grading scale, grade F is a fail.
Department og Biological Sciences, e-mail: firstname.lastname@example.org
For written exams, please note that the start time may change from 09:00 to 15:00 or vice versa until 14 days prior to the exam. The exam location will be published 14 days prior to the exam. Candidates must check their room allocation on Studentweb 3 days prior to the exam.
Type of assessment: Written eksamination
- 27.09.2019, 09:00
- 4 hours
- Withdrawal deadline
- Examination system
- Digital exam
- Solheimsgt. 18 (Administrasjonsbygget), Eksamenslokale 3. etg.