Unknown

Dataset Information

0

Multiple barriers in forced rupture of protein complexes.


ABSTRACT: Curvatures in the most probable rupture force (f*) versus log-loading rate (log r(f)) observed in dynamic force spectroscopy (DFS) on biomolecular complexes are interpreted using a one-dimensional free energy profile with multiple barriers or a single barrier with force-dependent transition state. Here, we provide a criterion to select one scenario over another. If the rupture dynamics occurs by crossing a single barrier in a physical free energy profile describing unbinding, the exponent ν, from (1 - f*/f(c))(1/ν) ~ (log r(f)) with f(c) being a critical force in the absence of force, is restricted to 0.5 ≤ ν ≤ 1. For biotin-ligand complexes and leukocyte-associated antigen-1 bound to intercellular adhesion molecules, which display large curvature in the DFS data, fits to experimental data yield ν < 0.5, suggesting that if ligand unbinding is assumed to proceed along one-dimensional pulling coordinate, the dynamics should occur in a energy landscape with multiple-barriers.

SUBMITTER: Hyeon C 

PROVIDER: S-EPMC3422331 | biostudies-other | 2012 Aug

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC5842080 | biostudies-literature
| S-EPMC2928789 | biostudies-literature
2022-03-07 | GSE155971 | GEO
| S-EPMC3370124 | biostudies-literature
2016-12-15 | GSE83123 | GEO
2022-03-07 | GSE196497 | GEO
2021-08-17 | GSE181533 | GEO
| S-EPMC2592557 | biostudies-literature
| S-EPMC5860626 | biostudies-literature
| S-EPMC6733033 | biostudies-literature