Main, Ewan (2003) The folding and design of repeat proteins: reaching a consensus. Current Opinion in Structural Biology, 13 (4). pp. 482-9. ISSN 0959440X
Full text not available from this repository.Abstract
Although they are widely distributed across kingdoms and are involved in a myriad of essential processes, until recently, repeat proteins have received little attention in comparison to globular proteins. As the name indicates, repeat proteins contain strings of tandem repeats of a basic structural element. In this respect, their construction is quite different from that of globular proteins, in which sequentially distant elements coalesce to form the protein. The different families of repeat proteins use their diverse scaffolds to present highly specific binding surfaces through which protein-protein interactions are mediated. Recent studies seek to understand the stability, folding and design of this important class of proteins.
Item Type: | Article |
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Schools and Departments: | School of Life Sciences > Chemistry |
Depositing User: | Ewan Main |
Date Deposited: | 06 Feb 2012 18:35 |
Last Modified: | 31 May 2012 14:18 |
URI: | http://sro.sussex.ac.uk/id/eprint/17271 |