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The evolution of specificity in large protein families

Thornton, Janet M. and Favia, A.D. and Nobeli, Irilenia and Furnham, N. (2008) The evolution of specificity in large protein families. In: 33rd FEBS Congress & 11th IUBMB Conference: Biochemistry of Cell Regulation, June 28-July 3 2008, Athens, Greece.

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Official URL: http://dx.doi.org/10.1111/j.1742-4658.2008.06445.x

Abstract

Understanding the relationship between protein structure and biological function has long been a major goal of structural biology. With the advent of many structural genomics projects, there is a practical need for tools to analyse and characterise the possible functional attributes for a new structure. One of the major challenges in assigning function is to recognise a cognate ligand which may be a small molecule or a large macromolecule. At EBI we have been developing a range of methods which seek to annotate a functional site. These methods have some success dependent upon the shape and flexibility of the binding site. In this presentation I will review our progress in this area and describe application to two large families – the sulpher transferases (1) and the short chain ehydrogenase/reductases (2).

Item Type: Conference or Workshop Item (Lecture)
Additional Information: Lecture abstract only
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 04 Aug 2010 14:09
Last Modified: 17 Apr 2013 12:17
URI: http://eprints.bbk.ac.uk/id/eprint/990

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