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Lipid monolayer structure and intera...

Freites, Juan Alfredo.

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Lipid monolayer structure and interactions in the presence of peptides and proteins.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Lipid monolayer structure and interactions in the presence of peptides and proteins./
作者:	Freites, Juan Alfredo.
面頁冊數:	178 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4076.
Contained By:	Dissertation Abstracts International65-08B.
標題:	Physics, Condensed Matter. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3142939
ISBN:	0496010085

Lipid monolayer structure and interactions in the presence of peptides and proteins.
Freites, Juan Alfredo.

Lipid monolayer structure and interactions in the presence of peptides and proteins. - 178 p.

Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4076.

Thesis (Ph.D.)--University of California, Irvine, 2004.

Structural aspects of two simple model systems, protein-lipid monolayer and peptide-lipid monolayer, were studied by experimental and computer simulation techniques. In both cases, both the choice of system and the approach employed to studying it, were motivated by specific biological problems.

ISBN: 0496010085Subjects--Topical Terms:

1018743
Physics, Condensed Matter.

Lipid monolayer structure and interactions in the presence of peptides and proteins.
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245 1 0 $a Lipid monolayer structure and interactions in the presence of peptides and proteins.
300 $a 178 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4076.
500 $a Chair: Michael B. Dennin.
502 $a Thesis (Ph.D.)--University of California, Irvine, 2004.
520 $a Structural aspects of two simple model systems, protein-lipid monolayer and peptide-lipid monolayer, were studied by experimental and computer simulation techniques. In both cases, both the choice of system and the approach employed to studying it, were motivated by specific biological problems.
520 $a The interaction of annexin A1 with monolayers of dipalmitoylphosphatidylcholine (DPPC) was studied by fluorescence microscopy as a function of lipid monolayer phase and pH. It was shown that the annexin A1-DPPC interaction depends strongly on both the domain structure and phase behavior of the DPPC monolayer, and only weakly on the subphase pH. Annexin A1 was found to be line-active, adsorbing preferentially at phase boundaries. Also, annexin A1 was found to form networks in the presence of a domain structure in the lipid monolayer.
520 $a Molecular dynamics simulations were carried out on a model system composed of a surfactant protein B peptide, SP-B1--25, and a monolayer of hexadecanoic acid. A detailed structural characterization was performed as a function of the lipid monolayer specic area. It was found that the peptide remains inserted in the monolayer up to values of specific area corresponding to an untilted condensed phase of the pure hexadecanoic acid monolayer. The system remains stable by altering the conformational order of both the anionic lipid monolayer and the peptide secondary structure, and effectively constitutes a unique disordered lipid-peptide monolayer phase. Two elements appear to be key for the constitution of this phase: an electrostatic interaction between the cationic residues of the peptide with the anionic headgroups of the lipids, and an exclusion of the aromatic residues on the hydrophobic end of the peptide from the hydrophilic and aqueous regions of the system.
520 $a A direct comparison between molecular dynamics simulations and laboratory experiments was performed for hexadecanoic acid monolayer systems. In order to simulate specific points on the surface pressure vs. area isotherm, an algorithm for the control of surface pressure was developed based on previous work by Martyna, Tobias and Klein. The algorithm was implemented and tested with the hexadecanoic acid monolayer system.
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650 4 $a Physics, Condensed Matter. $3 1018743
650 4 $a Biophysics, General. $3 1019105
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790 1 0 $a Dennin, Michael B., $e advisor
790 $a 0030
791 $a Ph.D.
792 $a 2004
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