The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.

ABSTRACT: The F-actin crosslinker filamin from Dictyostelium discoideum (ddFLN) has a rod domain consisting of six structurally similar immunoglobulin domains. When subjected to a stretching force, domain 4 unfolds at a lower force than all the other domains in the chain. Moreover, this domain shows a stable intermediate along its mechanical unfolding pathway. We have developed a mechanical single-molecule analogue to a double-jump stopped-flow experiment to investigate the folding kinetics and pathway of this domain. We show that an obligatory and productive intermediate also occurs on the folding pathway of the domain. Identical mechanical properties suggest that the unfolding and refolding intermediates are closely related. The folding process can be divided into two consecutive steps: in the fir

SUBMITTER: Schwaiger I 

PROVIDER: S-EPMC1299227 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature