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Thermotropic behavior of lipid domai...
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Leidy, Chad.
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Thermotropic behavior of lipid domains in model membranes.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Thermotropic behavior of lipid domains in model membranes./
作者:
Leidy, Chad.
面頁冊數:
166 p.
附註:
Source: Dissertation Abstracts International, Volume: 63-09, Section: B, page: 4085.
Contained By:
Dissertation Abstracts International63-09B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3065272
ISBN:
0493841865
Thermotropic behavior of lipid domains in model membranes.
Leidy, Chad.
Thermotropic behavior of lipid domains in model membranes.
- 166 p.
Source: Dissertation Abstracts International, Volume: 63-09, Section: B, page: 4085.
Thesis (Ph.D.)--University of California, Davis, 2002.
Multi-component lipid bilayer membranes can have several lipid phases coexisting at a given temperature, which can lead to the formation of a domain structure. Temperature plays a crucial role in modulating this lipid domain structure. A binary mixture containing two lipid components with different melting temperatures can present a domain structure of gel and liquid-crystalline phases within a temperature range intermediate to the melting temperatures of the components. This domain structure will vary drastically in scale and shape with changes in temperature, which can have important implications for cells. Cell membranes are heterogeneous mixtures of lipid components. It has become evident that lipid domain structures that are present in cellular membranes play important roles in several key cellular processes. Obtaining a clearer understanding on the thermotropic behavior of lipid domain structures in multicomponent model membranes can provide useful insight into the role of lipid domain formation in cells.
ISBN: 0493841865Subjects--Topical Terms:
1017686
Biology, Cell.
Thermotropic behavior of lipid domains in model membranes.
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Multi-component lipid bilayer membranes can have several lipid phases coexisting at a given temperature, which can lead to the formation of a domain structure. Temperature plays a crucial role in modulating this lipid domain structure. A binary mixture containing two lipid components with different melting temperatures can present a domain structure of gel and liquid-crystalline phases within a temperature range intermediate to the melting temperatures of the components. This domain structure will vary drastically in scale and shape with changes in temperature, which can have important implications for cells. Cell membranes are heterogeneous mixtures of lipid components. It has become evident that lipid domain structures that are present in cellular membranes play important roles in several key cellular processes. Obtaining a clearer understanding on the thermotropic behavior of lipid domain structures in multicomponent model membranes can provide useful insight into the role of lipid domain formation in cells.
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The thermotropic behavior of lipid domain formation in a 1:1 DMPC/DSPC system is analyzed by monitoring the segregation of donor and acceptor fluorescent probes into coexisting gel and liquid-crystalline domains. The results reveal that a dynamic and fluctuation nanoscale gel/liquid-crystalline domain structure forms at two distinct temperatures, which correspond to the melting of DMPC-enriched and DSPC-enriched lipid domains. The results provide a clearer understanding of domain formation dynamics in multi-component bilayer membranes.
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Atomic force microscopy (AFM) on supported double bilayers is used to show the presence of the fluid-phase/ordered-phase domain structure at various temperatures for a 1:1 DMPC/DSPC system. The AFM results reveal the importance of ripple phase in defining this domain structure. In addition, the results establish a method for studying lipid domain formation with the use of supported double bilayers.
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Fourier transform infrared spectroscopy (FTIR) is used to asses the role of cholesterol in the thermotropic phase behavior of a 1:1 POPC/Sphingomyelin system. This is done in order to model the lipid phase behavior in the platelet membranes, and to explain the process of cold-induced activation of platelets, which is likely driven by a reorganization of the lipid domain structure.
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