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Biophysical Journal 71: 1605-1610 (1996)
© 1996 the Biophysical Society

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Stability of the dystrophin rod domain fold: evidence for nested repeating units.

R Calvert, E Kahana and W B Gratzer

Medical Research Council Muscle and Cell Motility Unit, King's College, London, UK.

ABSTRACT

An examination of fragments of the human dystrophin rod domain, corresponding to a single structural repeating unit, showed that a critical chain length, defined with a precision of one residue at the C-terminal end, is required for formation of the native tertiary fold. We report here that extending the chain by six residues beyond this minimum results in a large increase in conformational stability. This is not related to a change in association state of the polypeptide. The results support the conjecture that successive repeating units in the rod domain of the spectrinlike proteins form a nested structure, in which the N-terminal part of the three-helix bundle of one repeat packs into the overlapping structure of the preceding repeat. This would be expected to affect functional characteristics related to flexibility of the dystrophin rod domain.




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