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-capacityhttps://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:

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.

Content:

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:

Knowledge

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

Skills

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 https://www.uib.no/en/course/MOL310MOL310 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.

General competence

The student has

• the ability to place concepts discussed in https://www.uib.no/en/course/MOL310MOL310 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

Mandatory attendance to orientation meeting about written assignments.

Obligatory activities are valid for total six semesters.

The first lecture/orientation meeting is compulsory.

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