text: With double-stranded DNA, both Clausen-Schaumann et al. (2000) and Williams et al. (2001) showed that temperature melts and softens the bonds between the strands. A helical linker between spectrin repeats is qualitatively different from the repeats themselves in that the linker lacks any adjacent helices to interact with. Intramolecular hydrogen-bonding studies by Ragone (2001) indeed provide evidence that side-chain-to-side-chain interactions provide stabilizing contributions to helical structures. In a study of ionic strength effects on the thermal unfolding of spectrin peptides, Lusitani et al. (1998) also suggested that inter-repeat regions are less stable and more vulnerable to ionic strength effects which account for strong conformational changes under different ionic strengths.