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Diffraction studies of fluid lipid b...

The Johns Hopkins University.

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Diffraction studies of fluid lipid bilayers with membrane proteins.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Diffraction studies of fluid lipid bilayers with membrane proteins./
作者:	Han, Xue.
面頁冊數:	222 p.
附註:	Adviser: Kalina Hristova.
Contained By:	Dissertation Abstracts International69-04B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3309666
ISBN:	9780549583530

Diffraction studies of fluid lipid bilayers with membrane proteins.
Han, Xue.

Diffraction studies of fluid lipid bilayers with membrane proteins. - 222 p.

Adviser: Kalina Hristova.

Thesis (Ph.D.)--The Johns Hopkins University, 2008.

In summary, neutron diffraction can provide unique structural information and new insights into membrane structure and membrane protein topology.

ISBN: 9780549583530Subjects--Topical Terms:

1019105
Biophysics, General.

Diffraction studies of fluid lipid bilayers with membrane proteins.
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035 $a (UMI)AAI3309666
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100 1 $a Han, Xue. $3 1023275
245 1 0 $a Diffraction studies of fluid lipid bilayers with membrane proteins.
300 $a 222 p.
500 $a Adviser: Kalina Hristova.
500 $a Source: Dissertation Abstracts International, Volume: 69-04, Section: B, page: 2167.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2008.
520 $a In summary, neutron diffraction can provide unique structural information and new insights into membrane structure and membrane protein topology.
520 $a The folding of membrane proteins occurs in the context of the highly anisotropic lipid bilayer. Membrane protein topology, given by the disposition of the transmembrane (TM) segments relative to the lipid bilayer, is determined by lipid-protein and protein-protein interactions. Direct structural information about the topology, as well as the response of the membrane to the presence of proteins, is important for describing the interactions at the molecular level. In this dissertation, diffraction was used to determine protein topology by measuring the depth of penetration of amino acids of (1) an alpha-helical peptide (the TM domain of fibroblast growth factor receptor 3 (FGFR3)), (2) a beta-sheet hexapeptide (AcWL5), and (3) an unstructured peptide (AcWL 4). Also, the insertion of arginine residues in bilayers and the hydrocarbon core (HC) response to the inserted arginines was investigated.
520 $a The alpha-helical peptide studied is the TM domain of FGFR3, a receptor tyrosine kinase which conducts biochemical signals across the plasma membrane. The Gly380Arg mutation in FGFR3 TM domain causes achondroplasia, the most common form of human dwarfism. Neutron diffraction was used to determine the disposition of FGFR3 TM domain in fluid lipid bilayers and to investigate whether the Gly380Arg mutation affects the topology of the protein in the bilayer. The results demonstrate that, in a model system, the Gly380Arg mutation induces a shift in the membrane-embedded segment. The center of the hydrocarbon core-embedded segment in the mutant is close to the mid-point between Arg380 and Arg397. This finding furthers our knowledge about basic amino acid insertion into bilayers and may lead to new insights into the pathogenesis in achondroplasia.
520 $a The neutron diffraction studies were extended to unstructured and beta-sheet peptides. AcWL4 is an unstructured peptide and it is expected to reside in the interfacial region of the lipid bilayer as a monomer. On the other hand, AcWL5 has been shown to assemble cooperatively into beta sheet aggregates in lipid bilayers. Neutron diffraction was used to study the disposition of the peptides in bilayers. It was found that the deuterium labels in AcWL5 have no well-defined TM distribution, while AcWL 4 exhibits a well-defined interfacial location. Thus, the AcWL 5 oligomer must be a staggered TM beta-sheet, and its assembly must be dominated by protein-protein interactions rather than hydrophobic complimentarity. These results have implications for the structure and folding of proteins in their native membrane environment and highlight the importance of the interplay between hydrophobic complimentarity and protein-protein interactions in determining the structure of membrane proteins.
520 $a The presence of arginines in lipid bilayers is expected to perturb the bilayer structure. Arg380 in the mutant FGFR3 TM domain is buried in the hydrocarbon core of the bilayer, positioned at about 11 A from the bilayer center; a second arginine, Arg397, is located at 13 A from the bilayer center. Long range bilayer distortions due to the buried Arg380 and Arg397 were investigated, using neutron diffraction and specific deuteration of the acyl chains. This was accomplished by characterizing the HC distribution in the presence of both wild-type and mutant FGFR3 TM domains, such that the effect of the mutation can be directly addressed. The results show that HC perturbations due to the achondroplasia mutation do not propagate beyond the immediate vicinity of the peptide, and highlight the ability of the bilayer to accommodate basic amino acids without long range perturbations.
590 $a School code: 0098.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 69-04B.
790 $a 0098
790 1 0 $a Hristova, Kalina, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3309666