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An Introduction To Protein Science

University of Oxford , Oxford ,England
7 - 8 September 1999

Invited Speakers: Dr David Harris (Course Director) read Biochemistry at Oxford University and conducted his post-doctoral work in Amsterdam before returning to Oxford. After lecturing at Leeds University he returned to Oxford once more and is currently a lecturer in Biochemistry.

Dr Mark Sansom studied as an undergraduate in Biochemistry at Oxford University moving into Molecular Biophysics for post-graduate work. In 1991 he returned from Nottingham University - where he had been lecturing in Zoology - to take up a lectureship at Oxford in Biochemistry and he is currently a University reader in Biochemistry.

DNA is renowned as the blueprint for life. However, just as a blueprint itself cannot perform tasks or build structures, DNA itself does not carry out the processes of life; these are carried out almost entirely by protein molecules, which make up the structures and molecular machines that make the cell function.
It is the unique chemical and physical properties of proteins that give them their biological functions. Proteins are macromolecules made up from only 20 building blocks – the amino acids – but their size and complexity endows them with an almost infinite range of desirable properties, such as self assembly, molecular recognition and catalysis. These properties are a summation of the chemical properties of the individual amino acids, overlaid with series of non-covalent interactions leading to the molecule adopting a specific and complex 3-dimensional conformation.
It is the aim of the course to elucidate the links between the chemical structure of proteins and their conformational and functional properties, and to show how, despite the apparent complexities, patterns are currently emerging that allow us to understand and predict protein structures. It explains how this knowledge can be used to help us to isolate and identify proteins, and adapt them for our own use, both outside the body (in diagnostics or industrial catalysts) and within it (as potential drugs).

Who should find it valuable?
For many years, the structure and properties of proteins have been of interest to those involved in drug design – a drug typically being a small molecule that interacts with a specific protein target. Today, proteins (particularly antibodies and hormones) are being used as drugs themselves. Both of these approaches exploit the exquisite specificity of protein structure and action, but the second also opens up questions as to how to produce these proteins in large amounts, how quality of the preparation can be assessed and maintained, and how the labile conformation of the active protein can be compatible with a suitable shelf life and drug formulation. In addition, proteins might seem to be the ideal industrial catalysts, in that they can catalyse reactions regio- and stereospecifically at nearly diffusion limited rates. How can they do this? Can we actually use enzymes industrially, or are they too labile to survive in industrial plants? Anyone interested in any of these questions should find this course useful.

Programme: Proteins – structure and applications
1. Protein Structure Basics
· Amino acids, peptides and proteins
· Local conformation – the Ramachandran plot
· Secondary structure – regularity within proteins
· Tertiary structure – folding the backbone
· Domains and modules

2. Protein Folds
· Databases of protein stucture – displaying folds
· All a folds e.g. 4 helix bundles. ‘Synthetic proteins’
· All b folds e.g retinol binding protein
· a/b folds – e.g.the TIM barrel and a+b folds – e.g. lysozyme
· multidomain proteins e.g. pyruvate kinase

3. Chemically modified proteins
· Chemical properties of amino acid side chains
· Directed protein modifiers as drugs – affinity labels and suicide substrates
· Covalent modification of proteins as a means of control
· Glycosylation – sites of protein glycosylation and the existence of glycoforms

4. Purifying proteins
· Releasing proteins from cells and membranes
· Protein surfaces – exploiting their features in purification
· Genetic engineering of proteins for ease of purification
· Chromatography in aqueous media – size exclusion, ion exchange, hydrophobic interactions
· Exploiting protein specificity – the design of affinity matrices

5. Determination of protein structures
· Study of secondary structure using CD and FTIR
· Protein nmr – principles and applications
· X-ray crystallography of proteins – principles and applications
· Electron microscopy and atomic force microscopy
· Computational methods – homology modelling and secondary structure prediction

6. Protein stability and folding
· Structures on the edge - stability of the native state of proteins
· Folding, unfolding and refolding – experimental methods in vitro
· The molten globule state
· Folding in the cell and the role of chaperonins

7. Enzymes and catalysis
· Theories of catalysis – can an enzyme be a ‘perfect’ catalyst?
· The active site concept – catalytic groups and ‘push-pull’ catalysis
· Activation entropy and strain – why enzymes are more than just chemical catalysts
· Roles of the enzyme surface in catalysis

8. Membrane proteins
· Classification of membrane proteins
· X-ray and electron diffraction methods – problems and achievements
· From sequence to topology – bioinformatics in developing and testing model structures
· Spectroscopic approaches

9. Analytical techniques
· Electrophoresis in gels and capillaries.
· Isoelectric focussing. 2D electrophoresis in gels
· Proteomics – visualising and identifying individual proteins
· Antibody blotting, mass spectrometry and sequencing in protein identification.

10. Antibodies and their use in analysis
· Structure of the antibody molecule
· Generation of antibody diversity. Monoclonal and polyclonal antibodies.
· Antibodies in identification of proteins in tissues – immunocytochemistry
· Quantitative use of antibodies –heterogeneous (e.g. ELISA) and homogeneous assays
· Sensitivity and ease of use in antibody-based assays.

Registration :

Please register the following delegate for the course named below (for multiple registrations please use copies of theis form):
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First Name___________________________________________________________________
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Background: It is helpful for the course tutors to know the background of delegates; please could you provide the details listed below.

· Your main discipline (e.g. Biochemistry, Organic Chemistry, Molecular Biology, Pharmacology etc.)

· Your background (please circle) BSc/MSc/MD/PhD

University of Oxford, CPD Centre
67 St Giles
OX1 3LU or Fax the form to (+44) (0) 1865 288163

Places are limited so early registration by application form is strongly recommended. This will assure a place on the conference.
Registration by Fax or Mail:
Upon request, a place on the conference can be reserved for individuals who require time to obtain authorisation and process the payment of fees. This can be done by faxing or mailing the completed and signed application form to Rachel Bristow (Fax No: +44 (0)1865 288163). Invoices will be issued immediately to those submitting application forms only.
Please note that enrolments are made on a strictly first-come first-served basis, and therefore bookings will only be confirmed after a completed application form has been received. Note also that the organisers reserve the right to refuse admission to any delegate who has not paid the registration in full before the conference starts. In the event of late bookings, payment in full will be required at the registration on the first day of the conference or it is our policy to request credit card details which will be held for three weeks before processing or until payment is received.

Those who register by mail and have not received confirmation within three weeks should call us to ensure that their application has not been mislaid. Any delegate who has not received a confirmation of registration five days prior to the scheduled date of a conference should ring the CPD Centre to confirm that the conference will convene as scheduled.

The full conference fee covers tuition, notes, lunches and daytime refreshments.

PAYMENT: Payment can be made in several ways: By cheque: payable to the OUDCE in pounds sterling. By credit card: using VISA, ACCESS or MASTERCARD. We are not able to accept any other forms of credit card. By Bank Transfer: please inform us and we will send the appropriate details.

This Programme is financially self-supporting, and it is necessary to establish a minimum enrolment in each conference. If the conference is cancelled by the organisers, registered delegates will be given as much notice as possible (normally at least 10 days prior to the conference start-date). However, our liability will be limited to the refund of the registration fees in full (without deductions). If a registration is cancelled by a delegate, full refunds of registration fees less £50 administration costs are payable for cancellations received in writing ten working days before the conference starts. After this date no fees are returnable. The organisers reserve the right to make alterations to the stated Programme and other arrangements as deemed necessary.

Registered delegates who cannot attend the conference may be substituted at any time. Please notify Rachel Bristow at the address given below as far in advance as possible, giving full details of the person who will attend in your place. A completed application form for the replacement should thereafter be faxed to the CPD Centre.

FURTHER INFORMATION: Queries about any aspects of the programme - including registration, accommodation, fees, etc. - should be referred to either:
Rachel Bristow, CPD Administrative Assistant, E-mail: rachel.bristow@conted.ox.ac.uk, Tel: +44 (0)1865 288162
Suzy Hodge, CPD Portfolio Manager E-mail: suzy.hodge@conted.ox.ac.uk, Tel: +44 (0)1865 288167
Fax: +44 (0)1865 288163

University of Oxford, CPD Centre
67 St Giles

or Fax the completed form to the number above

Deadline for Abstracts: N/A

Email for Requests and Registration: cpdbio@contend.ox.ac.uk

Posted by: Suzy Hodge Host: mminchin.conted.ox.ac.uk date: April 28, 1999 10:44:53
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