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SUMMARY:On artificial cilia and nuclear pores : a solid mechanician going 
 bio
DTSTART:20121106T141500
DTEND:20121106T151500
DTSTAMP:20260509T052151Z
UID:3a36c973d342414910261a8adba008c86fbb1f4f8c5e09f7ffafe09a
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Patrick R. Onck\nIn this presentation I will discuss two
  recent research topics that are aimed at understanding and learning from 
 nature’s intriguing working principles. In the first topic\, we explore 
 a new way to propel fluids through micro-channels of lab-on-a-chip devices
  by mimicking the fluid transport mechanisms of natural ciliates\, such as
  Paramecia. Fluid propulsion of Paramecia takes place by means of hair-lik
 e motile appendages known as cilia that beat in an asymmetric manner. In a
 ddition\, the individual cilia beat out-of-phase which results in a wave-l
 ike motion (metachronal waves). Here\, we design magnetic artificial cilia
  that can be externally actuated to mimic these non-reciprocal deformation
 s (see Fig. 1). The artificial cilia can be realized using thin films cons
 isting of a polymer matrix filled with magnetic nano-particles\, allowing 
 actuation by means of an external magnetic field. We use a coupled magneto
 -mechanical solid-fluid model to explore the conditions at which a magneti
 c film will mimic the asymmetric motion of natural cilia. The response of 
 the artificial cilia is studied in terms of the dimensionless parameters t
 hat govern their physical behavior and identify the parameter space in whi
 ch the cilia can generate maximal flow.   In the second topic\, we explo
 re the transport properties of the nuclear pore complex (NPC)\, a giant mo
 lecular complex that provides directional\, fast and yet selective transpo
 rt of proteins across the nuclear envelope. Natively disordered proteins (
 FG-nups) that line the central channel of the NPC play a key role in regul
 ating the nuclear transport. The exact transport mechanism\, however\, is 
 still not clear. To obtain insight in this process we propose a coarse gra
 ined model to study the collective behavior of FG-Nups inside the transfer
  channel via molecular dynamics simulations (see Fig. 2). The obtained den
 sity plots reveal a unique distribution of charged and hydrophobic residue
 s inside the NPC. In addition\, we show that these distributions are encod
 ed in the specific amino-acid sequence of the FG-Nups.
LOCATION:ME B3 31 http://plan.epfl.ch/?room=MEB331
STATUS:CONFIRMED
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