Chapter category:

From artificial antibodies to nanosprings: the biophysical properties of repeat proteins

This chapter appears in the following book:

Protein Dimerization
(and Oligomerization) in Biology

Edited by: Jacqui Matthews
ISBN: TBA
» Get more information about this book at landesbioscience.com «

Chapter authors:
Laura S. Itzhaki and Alan R. Lowe

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In this chapter we review recent studies of repeat proteins, a class of proteins consisting of tandem arrays of small structural motifs that stack approximately linearly to produce elongated structures. We discuss the observation that, despite lacking the long‑range tertiary interactions that are thought to be the hallmark of globular protein stability, repeat proteins can be as stable and as coorperatively folded as their globular counterparts. The symmetry inherent in the structures of repeat arrays, however, means there can be many partly folded species (whether it be intermediates or transition states) that have similar stabilities. Consequently they do have distinct folding properties compared with globular proteins and these are manifest in their behaviour both at equilibrium and under kinetic conditions. Thus, when studying repeat proteins one appears to be probing a moving target: a relatively small perturbation, by mutation for example, can result in a shift to a different intermediate or transition state. The growing literature on these proteins illustrates how their modular architecture can be adapted to a remarkable array of biological and physical roles, both in vivo and in vitro. Further, their simple architecture makes them uniquely amenable to redesign—of their stability, folding and function—promising exciting possibilities for future research.

Laura S. Itzhaki
MRC Cancer Cell Unit, Hutchison-MRC Research Centre, Hills Road, Cambridge, UK

Alan R. Lowe

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Chapter category:

From artificial antibodies to nanosprings: the biophysical properties of repeat proteins

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