Multiple barriers in forced rupture of protein complexes

Details Multiple barriers in forced rupture of protein complexes Multiple barriers in forced rupture of protein complexes

2012-04-06

arxiv.org/abs/1204.1418v1

Physics

Biological Physics

8 pages, 5 figures

Scientific paper

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 $\nu$, from $(1- f^*/f_c)^{1/\nu}\sim(\log r_f)$ with $f_c$ being a critical force in the absence of force, is restricted to $0.5 \leq \nu \leq 1$. 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 $\nu<0.5$, suggesting that ligand unbinding is associated with multiple-barrier crossing.

Affiliated with

Also associated with

No associations

Rating

Multiple barriers in forced rupture of protein complexes does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Multiple barriers in forced rupture of protein complexes, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Multiple barriers in forced rupture of protein complexes will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-183281