Abstract
Repeat proteins contain tandem arrays of a small structural motif. In contrast to globular proteins, they are stabilized only by interactions between residues that are close in sequence. The modular structure of repeat proteins makes them ideal systems in which to study protein folding and stability. In this chapter, we review studies that enabled an understanding of key aspects of repeat protein stability and folding: the basis and limits of cooperativity, simple models to quantify and predict energy landscapes, and the connection between equilibrium stability and folding pathways. We also discuss the implications of these studies for the general understanding of protein folding.
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