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Lipid dynamics in the plasma membran...

Nishimura, Stefanie Y.

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Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking./
作者:	Nishimura, Stefanie Y.
面頁冊數:	261 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5997.
Contained By:	Dissertation Abstracts International66-11B.
標題:	Chemistry, Physical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197487
ISBN:	0542431858

Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking.
Nishimura, Stefanie Y.

Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking. - 261 p.

Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5997.

Thesis (Ph.D.)--Stanford University, 2006.

Single-molecule epifluorescence microscopy was used to observe the translational motion of glycosylphosphatidylinositol (GPI)-linked and transmembrane I-E k class II MHC membrane proteins in the plasma membrane of Chinese hamster ovary (CHO) cells. Biochemical studies suggested that these proteins may be confined to putative lipid microdomains in the plasma membrane. The individual I-Ek proteins were visualized with a Cy5-labeled peptide that binds with high affinity to a specific extracytoplasmic site common to both proteins. Single-molecule trajectories were used to compute diffusion coefficients and to search for deviation from Brownian motion. Analyses were employed to detect stable partitioning into either static or mobile domains, and both analyses showed that motion of the proteins was predominantly Brownian at room temperature.

ISBN: 0542431858Subjects--Topical Terms:

560527
Chemistry, Physical.

Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking.
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245 1 0 $a Lipid dynamics in the plasma membrane examined with single-molecule fluorescence tracking.
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500 $a Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5997.
500 $a Adviser: W. E. Moerner.
502 $a Thesis (Ph.D.)--Stanford University, 2006.
520 $a Single-molecule epifluorescence microscopy was used to observe the translational motion of glycosylphosphatidylinositol (GPI)-linked and transmembrane I-E k class II MHC membrane proteins in the plasma membrane of Chinese hamster ovary (CHO) cells. Biochemical studies suggested that these proteins may be confined to putative lipid microdomains in the plasma membrane. The individual I-Ek proteins were visualized with a Cy5-labeled peptide that binds with high affinity to a specific extracytoplasmic site common to both proteins. Single-molecule trajectories were used to compute diffusion coefficients and to search for deviation from Brownian motion. Analyses were employed to detect stable partitioning into either static or mobile domains, and both analyses showed that motion of the proteins was predominantly Brownian at room temperature.
520 $a Reduction of the total cell cholesterol concentration resulted in an approximately 6-fold decrease in the diffusion coefficient for the MHC class II proteins when imaged at room temperature. At 37°C, cholesterol depletion caused a smaller suppression of the diffusion for these proteins than was observed at 22°C (2-fold). Diffusion of MHC class II proteins was predominately Brownian at all studied cholesterol concentrations and temperatures. When the temperature was raised from 22 to 42°C, a change was detected at &sim;35°C in the activation energy for diffusion.
520 $a The diffusion of the fluorescent lipid analogs DiIC12, DiIC 18, and the slower population of Trite-DHPE also slowed upon cholesterol extraction. The diffusion of the DiI probes decreased to a lesser extent than was observed for the proteins. Cytoskeletal effects appear to be minimal. These results are consistent with the destruction of liquid cholesterol-phospholipid complexes upon cholesterol extraction resulting in solid-like high-melting point phospholipid domains that inhibit the lateral diffusion of membrane components.
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