Abstract

Analyses of genomes show that more than 70% of eukaryotic proteins are composed of multiple domains. However, most studies of protein folding focus on individual domains and do not consider how interactions between domains might affect folding. Here, we address this by analysing the three-dimensional structures of multidomain proteins that have been characterized experimentally and observe that where the interface is small and loosely packed, or unstructured, the folding of the domains is independent. Furthermore, recent studies indicate that multidomain proteins have evolved mechanisms to minimize the problems of interdomain misfolding.

Author affiliations

1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
2. University of Cambridge Department of Chemistry, MRC Centre for Protein Engineering, Lensfield Road, Cambridge CB2 1EW, UK.

Correspondence to: Sarah A. Teichmann¹ Email: sat@mrc-lmb.cam.ac.uk

Correspondence to: Jane Clarke² Email: jc162@cam.ac.uk

Published online 14 March 2007

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