Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.

ABSTRACT: The unfolding pathways of multiple-repeat spectrin molecules were examined using steered molecular dynamics (SMD) simulations to forcibly unfold double- and triple-repeat spectrin molecules. Although SMD has previously been used to study other repeating-domain proteins, spectrin offers a unique challenge in that the linker connecting repeat units has a definite secondary structure, that of an alpha-helix. Therefore, the boundary conditions imposed on a double- or triple-repeat spectrin must be carefully considered if any relationship to the real system is to be deduced. This was accomplished by imposing additional forces on the system which ensure that the terminal alpha-helices behave as if there were no free noncontiguous helical ends. The results of the SMD simulations highlight the imp

SUBMITTER: Paramore S 

PROVIDER: S-EPMC1614492 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature