Postgraduate Course: Protein Structure Determination (PGBI11021)

Course Outline
School	School of Biological Sciences	College	College of Science and Engineering
Credit level (Normal year taken)	SCQF Level 11 (Postgraduate)	Availability	Not available to visiting students
SCQF Credits	10	ECTS Credits	5
Summary	This course will deal with aspects of protein structure determination using multiple techniques including protein crystallography, nuclear magnetic resonance and electron microscopy.
Course description	This course gives an overview of the techniques used in protein structure determination, Protein X-Ray crystallography, Electron Microscopy and Nuclear Magnetic Resonance. The course deals with the physical details of the techniques used but also deals with the quality metrics used in structure reporting allowing students to assess the quality and reliability of a structure determination.

Entry Requirements (not applicable to Visiting Students)
Pre-requisites		Co-requisites
Prohibited Combinations		Other requirements	One year of University level Chemistry or Biochemistry. A knowledge of elementary Physics would be an advantage.
Additional Costs	None

Course Delivery Information

Academic year 2022/23, Not available to visiting students (SS1)		Quota: 38
Course Start	Semester 2
Timetable	Timetable
Learning and Teaching activities (Further Info)	Total Hours: 100 ( Lecture Hours 18, Seminar/Tutorial Hours 4, Programme Level Learning and Teaching Hours 2, Directed Learning and Independent Learning Hours 76 )
Assessment (Further Info)	Written Exam 0 %, Coursework 100 %, Practical Exam 0 %
Additional Information (Assessment)	1. Class Test (40%) 2. Essay (40%) 3. 10 minute presentation (20%)
Feedback	The class test combined with its associated feedback session illustrate to the students their level of understanding and use the increased understanding in the later essay/presentation assessment items of the course.
No Exam Information

Learning Outcomes
On completion of this course, the student will be able to: Describe the major techniques used for protein structure determination, and in more detail the use of X-Ray diffraction and Nuclear Magnetic resonance in macromolecular structural determination Understand methods of crystal preparation and X-ray data collection, X-ray data reduction, methods for phase determination, electron density map calculation and interpretation. Summarise methods for peak assignment and distance constraint determination in NMR. Give an overview of sample preparation and data collection in Electron Microscopy.