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Model for Self-Propulsive Helical Filaments: Kink-Pair Propagation
H. Wada and R.R. Netz
Phys. Rev. Lett. 99, 108102 (2007) (doi)

article in newscientist.com

Biology provides many examples of self-propelling microorganisms in the quasi-static low-Reynolds-number limit. Spiroplasma are tiny helical-shaped eubacteria lacking a rigid cell wall. They propel through viscous fluids by sending kinks or domain walls between regions of opposite handedness down their helical body. A simple elastic model for the domain-wall propagation is formulated and studied using hydrodynamic simulations and scaling arguments, giving good agreement with recent video-microscopy observations [J. Shaevitz, et al. Cell 122, 941 (2005)]. It is shown that the observed helical bacterial pitch angle Ψ ∼ 35° is optimized for maximal speed and efficiency.



Conference:
Modeling and Computer Simulations of Microswimming and Bacterial Motility
TU Munich, Garching (Munich) - 17-19.09.2007
Dr. V. Lobaskin, Prof. L. Bocquet and Prof. R.R. Netz


Shear-induced unfolding triggers adhesion of von Willebrand factor fibers
S.W. Schneider, S. Nuschele, A. Wixforth, C. Gorzelanny, A. Alexander-Katz, R.R. Netz, and M.F. Schneider
PNAS 104 (19), 7899-7903, (doi)

The behavior of a single collapsed polymer under shear flow is examined using hydrodynamic simulations and scaling arguments. Below a threshold shear rate γ* the chain remains collapsed and only deforms slightly, while above γ* the globule exhibits unfolding/refolding cycles. Hydrodynamics are crucial: in the free draining case γ scales with the globule radius R as γ ~ R^-1 , while in the presence of hydrodynamic interactions γ ~ R. Experiments on the globular von-Willebrand protein confirm the presence of an unfolding transition at a well-defined critical shear rate. These findings explain the function of the von-Willebrand factor, a protein present in our circulatory system, to stop bleeding under high shear-stress conditions as found in small blood vessels.

Shear-flow induced unfolding of polymeric globules
(Phys. Rev. Lett. 97, 138101 (2006), doi )
(A. Katz, R.R. Netz et al.)