Level of Study
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. Students will learn how to determine structures, analyze them, and understand their biological and biomolecular properties. There will be an emphasize on how several biomacromolecules assembles into functional assemblies and how these give rise to properties important for cells or the organisms.
The primary biomolecular focus of the course will be proteins. Other biomolecules and assemblies of biomolecule will generally only be discussed in connection with their relationship to proteins. 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. The course will offer introductions into relevant methodology, in particular how protein structures are determined experimentally and by computational techniques. 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 also discuss the structural and biochemical basis of molecular signaling, as well as enzyme function. Protein evolution from as sequence and structural perspective will be covered.
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 provide detailed explanations about
- forces and effects that leads to the formation of protein structure, and the different levels of protein structure, from the amino-acid level to larger, quaternary complexes
- how a protein uses its structural organization to achieve traits that do not occur in its individual components
- protein classification by structure and function
- 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
- Cryo-EM, NMR, X-ray diffraction and computational techniques for determining structure.
- Other relevant methodology to study protein fold, stability and function
- how evolution act on protein primary sequence and structure
The student is able to
- analyze structure-function relationships when presented with biological and structural information
- 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 macropmolecular problem
- orient themselves in the spatial- and temporal scale that is associated with macromolecular understanding (that is, Ångstrøm to nanometers, ps-ms)
- solve 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 existing 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, understand and make use of content in The Protein Databank
- use scientific sources and tools to pursue and solve problems related to structural biology
Required Previous Knowledge
Bachelor's degree in molecular biology, or equivalent background.
Teaching and learning methods
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. Written exam counts 75 % and the written assignment 25 % of final grade. Due to coronavirus situation the exam spring semester 2020 will be digital written exam taken home. Exam time: 4,5 hours.
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
Due to the measures taken to avoid the spread of SARS-CoV-2, UiB is closed for teaching and assessment. As a consequence, the following changes is made to assessment spring semester 2021:
- Written home examination counts for 65% of the grade
- Assignments counts as 35% of the grade
Examination Support Material
Textbooks, teaching materials, own notaries and the internet are allowed during written school exams at home, together with simple calculator is equivalent to models specified in the faculty's rules. During school exams -home, it is not allowed to cooperate with fellow student (s) or others. Furthermore, it is important not to disturb fellow students during the exam.
The grading scale used is A to F. Grade A is the highest passing grade in the grading scale, grade F is a fail.
The reading list will be available within June 1st for the autumn semester and December 1st for the spring semester.
The Programme Committee is responsible for the coontent, structure and quality of the study programme and courses.
The faculty of Mathematics and Natural Sciences - department of Biological Sciences has responsibility for the course and programme.
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.
Type of assessment: To written eksamination
- Withdrawal deadline
Type of assessment: Written eksamination
- 28.09.2021, 09:00
- 4 hours
- Withdrawal deadline
- Examination system
- Digital exam