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DRPS : Course Catalogue : School of Chemistry : Chemistry

Undergraduate Course: Biophysical Chemistry Level 11 (CHEM11016)

Course Outline
SchoolSchool of Chemistry CollegeCollege of Science and Engineering
Credit level (Normal year taken)SCQF Level 11 (Year 4 Undergraduate) AvailabilityAvailable to all students
SCQF Credits20 ECTS Credits10
SummaryThis is a course of lectures, tutorials and workshops that focuses on the interaction between key biological macromolecules and a wide range of fundamental physical phenomena. The course will describe the means by which these potentially highly informative interactions can be studied, and the data collected and processed. The subsequent exploitation of this data to infer key information concerning the three-dimensional structures, composition, dynamics, spatiotemporal distributions and mutual interactions of biological polymers such as proteins and nucleic acids will be outlined. The benefits to be gained from combined use of orthogonal but complementary techniques in an integrated fashion will be emphasized. The course will also teach how knowledge of the physical properties of biological polymers can be used to predict the way in which they fold, adopt quasi-stable tertiary structures and form complexes with other molecules.
Either the Level 10 or Level 11 version of this course version of this course (as specified in the degree programme tables) is a compulsory requirement for Year 4/5 students on degrees in Medicinal and Biological Chemistry, but can be taken by Year 4/5 students on any Chemistry degree programme.

Course description The course will emphasise the physical basis of each technique and how this relates to its limitations leading to an appreciation of why several experimental and computational techniques, applied in combination, provide the most robust information.

The course consists of a series of modules on the following topics: hydrodynamics i.e. the inference of molecular size, shape and association properties based on the movements of molecules with or in relation to aqueous solvent; the application of visible and ultra-violet light to studies of native biomolecules or biomolecules conjugated with chromophores or fluorophores (biophotonics); nuclear magnetic resonance (NMR) spectroscopy and its applications to structural and dynamic studies of proteins and protein complexes; X-ray crystallography and high-resolution structure determination of macromolecules; electron microscopy applied to biomacromolecules and composite biological structures; and the use of in silico techniques such as molecular dynamics and simulated annealing to predict the structure and behaviour of proteins based on an understanding of their physical properties.

Entry Requirements (not applicable to Visiting Students)
Pre-requisites Students MUST have passed: Chemistry 3A (CHEM09005) AND Chemistry 3B (CHEM09006) AND Chemistry 3P Practical and Transferable Skills (CHEM09007)
Prohibited Combinations Students MUST NOT also be taking Biophysical Chemistry Level 10 (CHEM10014)
Other requirements Must include a weighted average of Grade C or higher in all Chemistry 3 courses AND a weighted average of Grade D or higher in Chemistry 3A and Chemistry 3B, at the first attempt; or with the permission of Head of School.
Information for Visiting Students
High Demand Course? Yes
Course Delivery Information
Academic year 2015/16, Available to all students (SV1) Quota:  None
Course Start Semester 2
Timetable Timetable
Learning and Teaching activities (Further Info) Total Hours: 200 ( Lecture Hours 30, Seminar/Tutorial Hours 11, Summative Assessment Hours 3, Revision Session Hours 7, Programme Level Learning and Teaching Hours 4, Directed Learning and Independent Learning Hours 145 )
Assessment (Further Info) Written Exam 100 %, Coursework 0 %, Practical Exam 0 %
Additional Information (Assessment) One degree exam of 3 hours.

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Exam Information
Exam Diet Paper Name Hours & Minutes
Main Exam Diet S2 (April/May)3:00
Learning Outcomes
On completion of this course, the student will be able to:
  1. Demonstrate knowledge and understanding of the fundamental principles underlying the interplay between various physical phenomena and the physical properties of biomolecules, along with an awareness of the limitations of current understanding.
  2. Apply this knowledge and understanding to achieve a critical and nuanced appreciation of how the information needed to determine macromolecular structures and properties is acquired, processed, synthesised and assembled. 3) Generic Cognitive Skills
  3. Review the theory and practices of a range of biophysical techniques and demonstrate an ability to assess the robustness of the hypothetical models and mechanisms that are inferred from the data they generate, exercising an informed and critical judgement of the available data.
  4. Critically evaluate and understand the benefits as well as the theoretical and practical limitations of widely used software for simulating protein folding and protein-ligand interactions, and communicate the outcomes effectively.
  5. In workshops and small-group work collaborate with peers in self-learning exercises and share findings and informed judgements on protein folding predictions and the orthogonality of biophysical methods with the rest of the class.
Reading List
Additional Information
Graduate Attributes and Skills Not entered
Additional Class Delivery Information 27 hours lectures + 6 hours tutorials and two three-hour workshops, at times arranged.
Course organiserProf Paul Barlow
Tel: (0131 6)50 4727
Course secretaryMs Anne Brown
Tel: (0131 6)50 4754
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