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VERSION:2.0
CALSCALE:GREGORIAN
PRODID:UW-Madison-Physics-Events
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SEQUENCE:0
UID:UW-Physics-Event-3361
DTSTART:20140918T150000Z
DURATION:PT1H0M0S
DTSTAMP:20260419T161243Z
LAST-MODIFIED:20140908T125647Z
LOCATION:5310 Chamberlin Hall
SUMMARY:Continuum methods for understanding membrane protein stability
 \, R. G. Herb Condensed Matter Seminar\, Michael Grabe\, UC San Franci
 sco
DESCRIPTION:Experimental and computational studies have shown that cel
 lular membranes deform to stabilize the inclusion of transmembrane (TM
 ) proteins harboring charge. Recent analysis suggests that membrane be
 nding helps to expose charged and polar residues to the aqueous enviro
 nment and polar head groups. We previously used elasticity theory to i
 dentify membrane distortions that minimize the insertion of charged TM
  peptides into the membrane. Here\, we extend our work to consider the
  energetics of ion and small peptide penetration into the membrane as 
 well as large protein complexes. First\, we show that our continuum me
 thod accurately reproduces energy profiles and membrane shapes generat
 ed from molecular simulations of bare ion permeation at a fraction of 
 the computational cost. Importantly\, we find that the energetics of m
 embrane deformation strongly depend on membrane patch size both for io
 ns and peptides. Finally\, we present experimental and theoretical ana
 lysis that suggests that the antibacterial protein RegIIIa\, a C-type 
 lectin\, forms channel like complexes that disrupt cellular homeostasi
 s by inserting into membranes containing anionic lipids. We believe th
 at our work presents a novel\, computationally efficient method to sim
 ulate the effects of small molecules\, peptides and large complexes wi
 th the membrane.
URL:https://www.physics.wisc.edu/events/?id=3361
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