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PEDS Advance Access originally published online on June 18, 2004
Protein Engineering Design and Selection 2004 17(5):443-453; doi:10.1093/protein/gzh052
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Protein Engineering, Design & Selection vol. 17 no. 5 © Oxford University Press 2004; all rights reserved

The importance of loop length in the folding of an immunoglobulin domain

Caroline F. Wright, John Christodoulou, Christopher M. Dobson and Jane Clarke1

University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK

1 To whom correspondence should be addressed. E-mail: jc162{at}cam.ac.uk

Immunoglobulin (Ig)-like proteins have been shown to fold following formation of a nucleus comprising interactions between residues that are distant in the primary sequence. What role do the loops connecting these nucleus residues play? Here, the importance of loops connecting ß-strands in different sheets of the Ig fold is investigated, by insertion of five glycine residues into the B–C loop of an Ig domain from human titin, TI I27. The folding pathway of this elongated ‘pseudo wild-type’ TI I27 is probed using protein engineering and {Phi}-value analysis. The {Phi}-values calculated for mutants within the pseudo wild-type protein indicate that the folding nucleus in wild-type TI I27 is conserved, supporting the hypothesis that the inter-sheet loop is not critical to the formation of a long-range folding nucleus.

Received March 1, 2004; revised May 21, 2004; accepted May 24, 2004.

Edited by Susan Marqusee


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