MSc in Biomolecular Organisation

A part-time evening course

Course Tutors:
Dr J. E. Pitts
Dr Uma Bhattacharya

Department of Crystallography, Birkbeck College, Malet Street London, WC1E 7HX

Tel: 0171 631 6800

Introduction

The course focuses on recent developments in the areas of biochemistry, biophysics and molecular biology, which provide insight into the organisation and biological roles of subcellular components at the macromolecular and supramolecular level. The first part of the course introduces modern techniques such as recombinant DNA, protein engineering, X-ray crystallography, nuclear magnetic resonance and electron microscopy. The latter part of the course examines subcellular interactions of proteins and nucleic acids together with their biological roles, including chromatin, ribosomes, membranes, receptors, viruses and multienzyme complexes, emphasising protein, vaccine and drug design.

This is a two-year part-time course involving attendance on not more than three evenings per week in the first year, and one or two evenings per week plus a research project in the second year. Admission to the course is every two years, the next being October 1996.

Previous students have been employed in pharmaceutical companies, universities and medical physics laboratories.

This is a multidisciplinary MSc course taught principally by the Crystallography Department, with some teaching by lecturers in the Chemistry department.

The course covers several broad topics, described below:

  1. The genetic code, protein synthesis, genetic regulation, and gene mapping.
  2. Introduction to the use of X-ray diffraction in biology. Symmetry, structure determination of sugars, drugs, proteins, viruses and nucleic acids.
  3. Physical chemistry of macromolecules. Use of spectroscopic techniques such as nuclear magnetic resonance and circular dichroism.
  4. Electron microscopic studies of cells, organelles, viruses, fibres and macromolecular assemblies.
  5. Chemistry of biological building blocks, including saccharides, amino acids and peptides, nucleotides, sterols.
  6. Isolation, purification and biochemistry of proteins, polysaccharides and nucleic acids.
  7. Three-dimensional structure and function of proteins including allosteric enzymes, immunoglobulins, transport proteins, and polypeptide hormones.
  8. Organisation of proteins in membranes cell surface receptors.
  9. Supramolecular organisation of proteins and nucleic acids in chromatin, ribosomes, mRNA, tRNA and viruses.
  10. Cellular structure/morphology of mammalian, bacterial and plant cells. Organisation of cells into tissues, modification of cell form.
  11. The role of water in biological structure and organisation.

Course Synopsis

(Course timetable subject to change)

Term 1
Molecular Biology & Protein Engineering (Monday)
Intro to Diffraction Methods (Tuesday)
Biological Chemistry (Thursday)

Term 2
Protein Structure & Evolution (Monday)
Microscopy, Diffraction & Image Processing (Wednesday)
Dissertation study (Thursday)

Term 3
Dissertation Talks (Tuesday -June)
Computing for Molecular Biology (Wednesday - 8 weeks only)

Term 4
Molecular Biology of Complex Systems I (Tuesday)
Projects (Wednesday)
Biological Chemistry II (Thursday)

Term 5
Molecular Biology of Complex systems II (Tuesday)
Projects (Wednesday)
Projects (Thursday)

Term 6
Biological NMR (Four lectures total - days vary)
Revision Lectures & Projects Talks (Wednesday)
Dissertations: to be submitted by the beginning July - 1st yr

Projects: to be submitted by end of July - 2nd yr

Examination:

Theory papers - Sept/Oct - 2nd yr (2x3 hr exams)
Orals - one month later (approx)
Recommended reading:
Principles of Biochemistry, Lehninger, Nelson & Cox, Worth Publishers (1993)
Biochemistry, L Stryer, W H Freeman & Co, NY (1995) 4th Edition
Introduction to Protein Structure, C I Branden and J Tooze, Garland Pub. Inc. NY/LON (1991)

CURRICULUM

1. Molecular Biology and Protein Engineering

This course describes the applications of molecular biology to protein engineering. The fundamental techniques involved include gene cloning, site-directed mutagenesis and heterologous expression. Towards the end of the course a number of case studies of engineered proteins are described including chymosin and insulin-like growth factor.

2. Introduction to Diffraction Methods

This course covers the techniques used for three dimensional structure analysis of biological macromolecules. The methods used for purification and crystallisation of proteins and determination of their molecular structures are described along with appropriate X-ray diffraction theory. The course ends with a tour of the laboratory and demonstrations of modern X-ray and molecular graphics equipment.

3. Biological Chemistry I and II

The structure, conformation and function of nucleic acids, polysaccharides, proteins and their monomer units, and other important biological molecules are discussed. Inorganic biochemistry includes discussions of metalloproteins, amino acid side- chains as ligands; haem and non-haem proteins and calcium in proteins.

In the second year the chemistry of polysaccharides, proteoglycans, glycoproteins, lipopolysaccharides and teichoic acids is discussed. There is an introduction to molecular toxicology of metals, the physical basis of electronic spectroscopy, vibrational spectroscopy and optical activity, as well as an introduction to NMR spectroscopy of biological macromolecule.

4. Proteins: Structure, Function and Evolution.

The secondary amd tertiary structures adopted by protein molecules depend primarily on their amino acid sequences. This course describes the interactions that stabilise the folded structures of proteins and our understanding of how the nascent polypeptide folds to its functional conformation. The detailed relationship between the structure and function of proteins is described with specific examples such as enzymes and membrane proteins. Engineering strategies for optimising stability and specificity of proteins are also outlined.

5. Microscopy, Diffraction and Image Processing

Transmission Electron Microscopy and Scanning Electron Microscopy are discussed and illustrated including biological sample preparation, microtomy, immunoEM, enzyme cytochemistry, autoradiography, cryo techniques, shadowing, freeze-fracture, high voltage EM, and stereology.

Two dimensional crystallization, electron diffraction, and three dimensional reconstruction of 2D crystalline arrays will be discussed. Comparison with medical imaging/computer-aided tomography and new developments in detectors and imaging plates will be discussed. Specific examples of membrane proteins, helical filaments and icosahedral virus analysis will be examined.

6.Computing for Molecular Biology

This is an eight week course covering the use of computing resources available on the internet and the WWW.

7. Biological NMR

Modern techniques of NMR as applied to inorganic biochemistry, and drug metabolism as well as topics in protein structure and clinical applications to toxicology.

8. Molecular Biology of Complex Systems I & II

This is a two-term course describing our current state of knowledge of the Biomolecular Organisation of a number of complex biological systems. It relies on the background material developed in the other units of the course for understanding the nature of interactions in important biological complexes such as ribosomes, chromatin, the cytoskeleton, collagen, photosynthetic system, lipoproteins, the eye lens, membranes, antibodies, vision, hormone receptors and viruses.

Course Work

Includes a dissertation (5,000 words) to be written in the first year, with an oral presentation in term 3. The student is required to examine the literature on a topic chosen in consultation with the course tutors.

Research Projects

A research project is undertaken in the second year. Students have the opportunity to gain first-hand experience of working in established research groups using specialized equipment and modern techniques.

Students may submit their own ideas for projects and these are frequently accepted, including projects to be undertaken at their place of work if appropriate. A number of projects have produced results which are publishable.

Examination Methods

This MSc course will be examined by:

  1. Two written three hour papers
  2. Assessment of course work
  3. A written report on the project
  4. An oral examination
The examinations will be held in September or October in the final year of study. Oral examinations take place about a month later.

Entry Qualifications

Applicants should have formal training in chemistry or the biological or medical sciences, with desirably, at least an elementary training in physics and mathematics. However, consideration will be given to candidates with degrees in other appropriate subjects.

Teaching Staff

Biomolecular Organisation is an interdisciplinary course, taught by the Departments of Crystallography and Chemistry.

Other Courses

The Crystallography Department also offers MSc courses in (i) Crystallography (full-time), and (ii) Molecular Modelling and Bioinformatics (biennial part-time, annual full-time). There is an extensive PhD training programme for both full and part-time students.

Birkbeck College

Birkbeck College was founded in 1823 and incorporated by Royal Charter in 1926 as one of the multi-faculty schools of the University of London. Over half of the College's students are postgraduates. It specialises in evening courses designed for part-time students. Hence lectures take place betwen 6-9pm on weekday evenings. College facilities such as the library, bar and nursery are open every weekday evening in order to provide support for working students.

Application forms

Should you decide to pursue your application please complete your application form as clearly as possible and return it to the Registry, Birkbeck College, Malet Street, London WC1E 7HX, tel: 0171 631 6390.