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

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