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Computer simulation studies of membr...

The University of Utah.

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Computer simulation studies of membrane remodeling by shear flow and N-BAR domain protein modules.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Computer simulation studies of membrane remodeling by shear flow and N-BAR domain protein modules./
作者:	Blood, Philip Douglas.
面頁冊數:	69 p.
附註:	Source: Dissertation Abstracts International, Volume: 69-06, Section: B, page: 3453.
Contained By:	Dissertation Abstracts International69-06B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3319151
ISBN:	9780549691778

Computer simulation studies of membrane remodeling by shear flow and N-BAR domain protein modules.
Blood, Philip Douglas.

Computer simulation studies of membrane remodeling by shear flow and N-BAR domain protein modules. - 69 p.

Source: Dissertation Abstracts International, Volume: 69-06, Section: B, page: 3453.

Thesis (Ph.D.)--The University of Utah, 2008.

Cellular membranes consist of assemblies of amphiphilic lipids held together by hydrophobic driving forces in a liquid crystalline state. Lipids can freely diffuse within the plane of the membrane, which can reorganize and remodel in response to external forces while still maintaining its basic structure. Membrane remodeling is central to the ability of cells to move, grow, transport materials, respond to external stimuli, and maintain homeostasis. Using molecular dynamics simulation, these studies examine in atomistic detail how biological membranes remodel in response to certain protein machinery and extracellular forces. The first study characterizes the planar membrane response to an imposed hydrodynamic shear flow. This shear flow causes the lipids to reorient in the flow field and increases both intramolecular and intermolecular lipid order. No increase in the rate of trans-gauche isomerization is observed. This suggests that experimentally observed increases in membrane fluidity due to shear flow are caused by long wavelength fluctuations of the lipid bilayer that are suppressed in this simulation. The other studies investigate how membrane remodeling protein modules known as N-BAR domains induce membrane curvature. These studies show that N-BAR domains induce local curvature that matches the intrinsic curvature of the positively-charged concave surface of the BAR domain. The BAR domain can bind at various angles on the membrane surface, which changes the intrinsic curvature of the surface facing the bilayer, and thus the degree of induced membrane curvature. This suggests a means by which BAR domains can respond to, interact with, and induce a range of local membrane curvatures. Subsequent studies find that the embedded N-terminal amphipathic helices do not contribute directly to the development of local curvature. Therefore, the observed curvature is likely due almost exclusively to the interaction of the negatively-charged lipids with the BAR domain concave surface. In these simulations, the N-terminal helices are primarily important as anchors which maintain the BAR domain close the membrane surface. In addition, charged loops at either end of the BAR domain must bind tightly to the lipid bilayer to stabilize the BAR domain on the membrane surface so that the charged concave surface can drive local curvature.

ISBN: 9780549691778Subjects--Topical Terms:

1019105
Biophysics, General.

Computer simulation studies of membrane remodeling by shear flow and N-BAR domain protein modules.
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