Undergraduate Course: Structures and Functions of Proteins 3 (BILG09015)
|School||School of Biological Sciences
||College||College of Science and Engineering
|Credit level (Normal year taken)||SCQF Level 9 (Year 3 Undergraduate)
||Availability||Available to all students
|Summary||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.
Information for Visiting Students
|Pre-requisites||Equivalent of the courses listed above
|High Demand Course?
Course Delivery Information
|Academic year 2022/23, Available to all students (SV1)
|Learning and Teaching activities (Further Info)
Lecture Hours 22,
Seminar/Tutorial Hours 10,
Supervised Practical/Workshop/Studio Hours 15,
Feedback/Feedforward Hours 1,
Summative Assessment Hours 2,
Programme Level Learning and Teaching Hours 4,
Directed Learning and Independent Learning Hours
|Assessment (Further Info)
|Additional Information (Assessment)
6 x Portfolio exercises 30%
Practical report 20%
4 x Assessed exercise for each block of teaching (best of 3 out of 4) 50%
||Summative assessment feedback is given by GradeMark. Furthermore feedback is given on the first half in time for feed-forward to the second half. The demonstrators in practical classes give informal feedback on student results. Exemplars are given for practical write-ups.
|No Exam Information
On completion of this course, the student will be able to:
- Describe the principles and practice of the experimental methods used to study the structures and dynamics of macromolecules and their assemblies and to characterise their functional properties and mechanisms of action. Chemical and physical principles that determine the structures of proteins and nucleic acids. Principles of the interactions of proteins with other molecules and ligands. Principles underlying the types of mechanism by which protein function can be regulated.
- Perform a range of biochemical measurements and analytical and preparative procedures accurately and reproducibly, and to be able to explain the theoretical bases of these techniques.
- Comprehend biochemical papers, to interpret data in figures and tables, to use search systems and indices to find related papers and details of experimental methods, and to abstract papers.
- Produce a concise written report of experimental work, containing tables and figures in which results are presented with a realistic assessment of precision and of the limitations of the procedures used and data obtained, and a discussion of the theoretical basis of the work.
|Graduate Attributes and Skills
||Knowledge and Understanding: All components of the course provide this to some degree but your lectures, in particular, offer an important framework upon which you can build attributes. This University considers itself to be a research-led Institution and you will be exposed to cutting edge information and ideas as you progress through your degree course. In SFP you will develop a comprehensive knowledge of key features and functions of major macromolecules and macromolecular assemblies and will see how these operate in a cellular context.
Research and Enquiry: These skills are enhanced by encouraging further reading of books, research papers and electronic materials, to embellish your lecture and practical material. They underpin assessed, in-course material such as the weekly portfolio.
Personal and Intellectual Autonomy: By reading and preparing materials for tutorial sessions, you will learn to synthesise your own views, develop reasoned arguments and refine scientific judgement. In addition, we encourage self-development through use of past papers and the in course assessment. Such skills enhance your capacity for life-long and independent learning.
Communication: This is a key attribute of all scientists and it is therefore important that you develop skills to interact constructively with others and convey knowledgeable and balanced scientific views. We specifically encourage and develop these skills in group tutorials.
Personal Effectiveness: The ability to organise and summarise your thoughts and material in a flexible and accessible way are core features that are required for personal effectiveness. Planning, time management and reflection are central to this. Of course these features also interlink with your personal and intellectual autonomy. By providing you with a timetable where key submission dates are highlighted, we are encouraging you to develop your effectiveness throughout the course. These same skills extend to other courses and also to your overall ability to maximise your achievement whilst studying at this University.
Technical and Practical Skills: In order to continue in a scientific career it is important that you not only understand the conceptual basis of how experiments are designed and carried out but also that you have the underpinning practical skills required for employability. Our course has a particularly heavy laboratory-based, experimental component which is designed to prepare your for this, as well as to assist you in your future Honours course projects. As part of your laboratory training skills in basic structural biology techniques including the computational analysis of structural data, are provided. The laboratory skills you develop from your practical sessions include critical observation, investigation and interpretation, careful recording, quantification and analysis, and should serve you well in any future employment.
|Additional Class Delivery Information
||Practicals - These take place in person (for those on-campus). Those attending remotely will have on-line material provided on Learn that will take them through each practical. All material will be available to all students. Should face-to-face teaching be stopped, all students will continue with the on-line material that will be provided.
Practicals (Computing) - These sessions follow on from the practicals. They will be in person but provision will be made for those studying remotely. Should face-to-face teaching be stopped, then we will default to on-line material.
Pymol - Should face-to-face teaching be stopped, these take place on-line only, in Collaborate.
Whole class sessions for each block. Lecture material will be delivered on-line with one whole class face-to-face session per week. Should face-to-face teaching stop, these will be delivered by Collaborate.
|Course organiser||Dr Paul McLaughlin
Tel: (0131 6)50 7060
|Course secretary||Mrs Carolyn Wilson
Tel: (0131 6)50 8651