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• W73052090 endingPage "166" @default.
• W73052090 startingPage "153" @default.
• W73052090 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." @default.
• W73052090 created "2016-06-24" @default.
• W73052090 creator A5016533330 @default.
• W73052090 creator A5052850050 @default.
• W73052090 date "2012-01-01" @default.
• W73052090 modified "2023-09-25" @default.
• W73052090 title "From Artificial Antibodies to Nanosprings" @default.
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• W73052090 doi "https://doi.org/10.1007/978-1-4614-3229-6_10" @default.
• W73052090 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22949117" @default.
• W73052090 hasPublicationYear "2012" @default.
• W73052090 type Work @default.

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