Course syllabus

Lecture courses: Available to current Oxford students only.

Year 2 (2020-21)

Year 3 (2021-22)

Revision

Course Leader

Professor Phil Biggin
Room 10-023, New Biochemistry
Telephone: 13305

Summary

In 1959 the first protein structure myoglobin was solved, followed by the structure of lysozyme in 1965. Both structures immediately indicated an explanation for biological function in terms of structure. Today there are over 100,000 structures of macromolecules in the data base solved by X-ray and NMR methods. Structural studies complemented by functional studies in solution and an understanding of chemistry provide unique insights into the roles of the individual components of the living cell. Genome analysis and advances in protein analysis have catalysed a series of paradigm changes in biology. Part of the course covers some areas of computational biochemistry and bioinformatics. These are now regularly used by experimentalists as well as by theoreticians in their own right.

The course comprises about 81 lectures, about 2/3 of which are in the second year. It is structured to provide a basic understanding of methods in the first part of the course. The later parts of the course are concerned with understanding biological and biochemical phenomena at the molecular level, some more advanced aspects of experimental approaches and understanding how to apply the techniques. The course co-ordinator is Professor Phil Biggin. He encourages comments on the course and is happy to discuss them with students. Undergraduates are also encouraged to attend the Biochemistry research seminars (Mondays at 4.00 pm) and biophysical seminars which are generally on Fridays at 11am.

The aims of this course are:

The material taught in each of the other papers of the Part I course will give you insight into biological problems that require a structural solution. In turn an understanding of the structural, biophysical and biochemical properties of macromolecules will help in understanding the biology.

  • To give you a basic understanding of the structures of biological macromolecules and the relationship between structure and biological function;
  • To introduce you to the experimental biophysical methods that are used to study macromolecules;
  • To introduce you to current methods in enzymology
  • To introduce you to the field of bioinformatics and to teach some of the tools for analysis of databases.

By the end of this course you should understand:

  • Methods used for the expression, purification and characterisation of proteins and an understanding of the chemical basis of the methods;
  • The physical methods used to study macromolecules including spectroscopic, NMR and X-ray and EM diffraction methods.
  • Approaches for studying the kinetic and chemical properties of enzymes and their reactions catalysed. Examples include a study of classical enzyme systems and some less familiar catalysts such as catalytic antibodies and catalytic RNA.
  • The classification of protein structures and the implications for the evolution and folding properties of properties of proteins;
  • The roles of metal ions in biological macromolecules and the relationship of chemical properties of metals to their biological roles;
  • Post-translational modification of proteins by glycosylation and the relationship of these modifications to proteins in health and disease;
  • The special properties of membrane proteins, the challenges they present to present day biochemistry and approaches used to study structure, topology and function. The relationship between structure and function in ion channels, membrane transporters, and neuro- transmitter receptors.
  • The concept of allosteric control and its role in regulation within the cell;
  • Protein/nucleic acid recognition with examples of both protein/DNA and protein/RNA interactions.

References

Relevant references for each course can be found on the course web pages