Structures and Functions of Proteins 3 (BILG09015)
Normal Year Taken
Delivery Session Year
Equivalent of the courses listed above
1. To describe the structures of biological macromolecules, particularly proteins, in relation to their functions in catalysis, ligand binding, membrane transport and ability to form and function as complexes, and to illustrate the types of experimental techniques used to study macromolecular structure and function. 2. To develop personal skills appropriate to a third-year biological science student, including competence in a range of laboratory techniques; the ability to analyse scientific papers; familiarity with the use of libraries and databases; the ability to present the results of experimental work concisely and accurately, both numerically and in writing, and to write about biochemical and molecular biological topics in a clear and well-organised manner.
How does protein structure and their dynamic properties work to produce the great range of physiological responses that we observe in cells? The course provides the basic groundwork necessary to equip a future Honours student in Biochemistry or Molecular Biology to answer this question. However, because of the rapid development of molecular studies and their growing importance in many areas of modern laboratory-based biology, the course is also designed to provide a strong background for students heading eventually for Biotechnology, Genetics, Immunology, or Pharmacology. The information in this course provides the basis for modern drug development strategies and an underpinning for the pharmaceutical industry. The emphasis is oriented towards development as a scientist and to making the transitions to Junior Honours. Experimental techniques and lectures are supplemented with workshops that reinforce this approach. An important feature of the in-course assessment is to introduce students to the scientific literature, both in terms of how to read and how to appraise critically original papers. Practicals provide hands-on experience of currently used laboratory techniques such as electrophoretic mobility shift assay, spectroscopy, electrophoresis, and protein chromatography; development of skills in experimental design and in handling quantitative data are particularly important. Molecular graphics and modelling software is introduced to allow easy manipulation and examination of complex molecules, in order to supplement practical, lecture and workshop material. There are four main themes in the lecture course: (i) Students are introduced to the types of quaternary structure, and their symmetries, that are found in biological complexes.(ii) Then there is an emphasis on how we find out about proteins: about how mass spectroscopy can be used to identity proteins, and to establish stoichiometry of complexes; about how X-ray crystallography, NMR, and cryo e-m are used to determine protein structures; and about how optical methods are used to follow dynamic properties, particularly those related to fluorescence, a major technique.(iii) The third theme is on quantitative analysis of the kinetics of protein:protein interactions and of reactions catalysed by proteins.(iv) The principles established in the first three themes are explored by looking at molecular machines, particularly those that are drug targets: G-coupled Protein Receptors and ion channels, with an introduction to membrane structure.
Written Exam 0%, Coursework 100%, Practical Exam 0%
Additional Assessment Information
In-course assessment:7 x Portfolio exercises (best 6 out of 7) 30%Practical report 20%4 x Assessed exercise for each block of teaching (best of 3 out of 4) 50%
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