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Phase transitions in two-dimensional...

Schief, William R., Jr.

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Phase transitions in two-dimensional model systems.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Phase transitions in two-dimensional model systems./
Author:	Schief, William R., Jr.
Description:	148 p.
Notes:	Chair: Viola Vogel.
Contained By:	Dissertation Abstracts International60-11B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9952897
ISBN:	0599557257

Phase transitions in two-dimensional model systems.
Schief, William R., Jr.

Phase transitions in two-dimensional model systems. - 148 p.

Chair: Viola Vogel.

Thesis (Ph.D.)--University of Washington, 1999.

Lipid and protein monolayers at the air/water interface are well suited for the study of two-dimensional phase transitions as their thermodynamic parameters may be tightly controlled, and they are amendable to in situ, non-perturbative, surface-analytical techniques. In this dissertation, quantitative light microscopy techniques are developed and expanded to study transitions in lipid and protein monolayers at the air/water interface. In the simplest model system studied, pure phospholipid monolayers, the introduction of light scattering microscopy reveals previously undetected, nanoscale topographic transitions in a microscopic pattern throughout the condensed phase. The findings demonstrate that condensed phospholipid phases are not flat as conventionally thought, and indicate that a patterned distribution of packing defects is imprinted on the monolayer during the first order liquid-to-condensed transition. As the monolayer is compressed, the pattern of defects persists in the pure condensed phase, giving rise to first a corrugation transition and later a budding transition. Finally, the pattern of defects controls the morphology of the monolayer collapse phase transition. The findings show the high sensitivity of light scattering microscopy to surface deformations on the angstrom to nanoscale and demonstrate the promise of this technique for future discoveries in a range of systems at fluid interfaces. In binary mixed monolayers of phospholipids and dihydrocholesterol and highly complex natural lung surfactant monolayers, quantitative Brewster angle microscopy leads to the discovery of a first order, two- to three-dimensional phase transition from monolayer to monolayer plus overlying bilayer discs. This phase transition occurs within the lower end of the physiological range of surface pressure, so the discovery raises new questions concerning the structure/function relationship of pulmonary surfactant and specifically points to a powerful structural impact by the component cholesterol. To answer fundamental physical questions concerning two-dimensional protein crystallization, a phenomena with diverse biotechnological applications, quantitative Brewster angle microscopy is extended to measure protein surface density at the air/water interface. The two-dimensional crystallization of the protein streptavidin underneath functionalized lipid monolayers is analyzed with regard to the surface protein density.

ISBN: 0599557257Subjects--Topical Terms:

1019105
Biophysics, General.

Phase transitions in two-dimensional model systems.
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005 20110505
008 110505s1999 eng d
020 $a 0599557257
035 $a (UnM)AAI9952897
035 $a AAI9952897
040 $a UnM $c UnM
100 1 $a Schief, William R., Jr. $3 1256378
245 1 0 $a Phase transitions in two-dimensional model systems.
300 $a 148 p.
500 $a Chair: Viola Vogel.
500 $a Source: Dissertation Abstracts International, Volume: 60-11, Section: B, page: 5579.
502 $a Thesis (Ph.D.)--University of Washington, 1999.
520 $a Lipid and protein monolayers at the air/water interface are well suited for the study of two-dimensional phase transitions as their thermodynamic parameters may be tightly controlled, and they are amendable to in situ, non-perturbative, surface-analytical techniques. In this dissertation, quantitative light microscopy techniques are developed and expanded to study transitions in lipid and protein monolayers at the air/water interface. In the simplest model system studied, pure phospholipid monolayers, the introduction of light scattering microscopy reveals previously undetected, nanoscale topographic transitions in a microscopic pattern throughout the condensed phase. The findings demonstrate that condensed phospholipid phases are not flat as conventionally thought, and indicate that a patterned distribution of packing defects is imprinted on the monolayer during the first order liquid-to-condensed transition. As the monolayer is compressed, the pattern of defects persists in the pure condensed phase, giving rise to first a corrugation transition and later a budding transition. Finally, the pattern of defects controls the morphology of the monolayer collapse phase transition. The findings show the high sensitivity of light scattering microscopy to surface deformations on the angstrom to nanoscale and demonstrate the promise of this technique for future discoveries in a range of systems at fluid interfaces. In binary mixed monolayers of phospholipids and dihydrocholesterol and highly complex natural lung surfactant monolayers, quantitative Brewster angle microscopy leads to the discovery of a first order, two- to three-dimensional phase transition from monolayer to monolayer plus overlying bilayer discs. This phase transition occurs within the lower end of the physiological range of surface pressure, so the discovery raises new questions concerning the structure/function relationship of pulmonary surfactant and specifically points to a powerful structural impact by the component cholesterol. To answer fundamental physical questions concerning two-dimensional protein crystallization, a phenomena with diverse biotechnological applications, quantitative Brewster angle microscopy is extended to measure protein surface density at the air/water interface. The two-dimensional crystallization of the protein streptavidin underneath functionalized lipid monolayers is analyzed with regard to the surface protein density.
590 $a School code: 0250.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Physics, Condensed Matter. $3 1018743
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690 $a 0611
690 $a 0786
710 2 0 $a University of Washington. $3 545923
773 0 $t Dissertation Abstracts International $g 60-11B.
790 $a 0250
790 1 0 $a Vogel, Viola, $e advisor
791 $a Ph.D.
792 $a 1999
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9952897