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Protein Dimerization and Oligomerization in Biology pp 153–166Cite as

From Artificial Antibodies to Nanosprings

The Biophysical Properties of Repeat Proteins

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 747))

Abstract

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 co-orperatively 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.

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Cambridge, Cambridge, UK

    Laura S. Itzhaki

  2. Department of Physics, University of California-Berkeley, Berkeley, California, USA

    Alan R. Lowe

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  1. Laura S. Itzhaki
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  2. Alan R. Lowe
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Correspondence to Laura S. Itzhaki .

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  1. School of Molecular Bioscience, University of Sydney, Sydney, Australia

    Jacqueline M. Matthews PhD

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Itzhaki, L.S., Lowe, A.R. (2012). From Artificial Antibodies to Nanosprings. In: Matthews, J.M. (eds) Protein Dimerization and Oligomerization in Biology. Advances in Experimental Medicine and Biology, vol 747. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3229-6_10

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