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Solid-state NMR studies of phospholi...

Lu, Jun-Xia.

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Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules./
Author:	Lu, Jun-Xia.
Description:	159 p.
Notes:	Adviser: Gary A. Lorigan.
Contained By:	Dissertation Abstracts International68-05B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3264645
ISBN:	9780549030195

Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules.
Lu, Jun-Xia.

Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules. - 159 p.

Adviser: Gary A. Lorigan.

Thesis (Ph.D.)--Miami University, 2007.

Cholesterol is commonly found in eukaryotic cell membranes and has implicated cellular functions. The synthetic peptide KIGAKI is a peripheral membrane protein that has greater antimicrobial activity than many natural-occurring antimicrobial peptides. Phospholamban (PLB) is an integral membrane protein that regulates the contraction and relaxation cycle of cardiac muscle cells in the heart by binding to Ca-ATPase. The three membrane-associated macromolecules and their interactions with the phospholipid membranes were studied.

ISBN: 9780549030195Subjects--Topical Terms:

586156
Chemistry, Analytical.

Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules.
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020 $a 9780549030195
035 $a (UMI)AAI3264645
035 $a AAI3264645
040 $a UMI $c UMI
100 1 $a Lu, Jun-Xia. $3 1263704
245 1 0 $a Solid-state NMR studies of phospholipid model membranes and membrane-associated macromolecules.
300 $a 159 p.
500 $a Adviser: Gary A. Lorigan.
500 $a Source: Dissertation Abstracts International, Volume: 68-05, Section: B, page: 3015.
502 $a Thesis (Ph.D.)--Miami University, 2007.
520 $a Cholesterol is commonly found in eukaryotic cell membranes and has implicated cellular functions. The synthetic peptide KIGAKI is a peripheral membrane protein that has greater antimicrobial activity than many natural-occurring antimicrobial peptides. Phospholamban (PLB) is an integral membrane protein that regulates the contraction and relaxation cycle of cardiac muscle cells in the heart by binding to Ca-ATPase. The three membrane-associated macromolecules and their interactions with the phospholipid membranes were studied.
520 $a The topology of magnetically oriented phospholipid bilayer model membranes (bicelles) was probed using a high-resolution 1H-13 C heteronuclear dipolar solid-state NMR spectroscopy (SAMMY). Three different membrane-associated molecules (cholesterol, KIGAKI and PLB) were incorporated into the bicelles. The effects of these molecules on the membrane topology were compared and the SAMMY technique proved to be a fast and promising way to detect the different modes of interaction of these membrane-associated molecules with the bicelle membrane lipids.
520 $a The effect of cholesterol on the bicelles was further studied utilizing both solid-state 2H NMR and the EPR spin labeling approach. The results indicate a higher molecular ordering of the lipids and a higher alignment transition temperature of the bicelles in the presence of cholesterol.
520 $a Antimicrobial peptides can interact directly with the bacterial membranes and disrupt the membranes without causing any harm to the host mammalian membranes. The interaction mechanism between KIGAKI and different membrane mimics with various lipid compositions was analyzed using solid-state 2H, 31P NMR and relaxation studies from the membrane perspective. The results suggested a carpet interaction mechanism for KIGAKI.
520 $a Uniform 15N-labeled PLB was expressed as a maltose fusion protein in E. coli. BL21 (RIL) (DE3) cells and purified with a combination of affinity chromatography and reverse phase C4 HPLC. Solid-state 15N NMR studies concluded that PLB has two populations with different dynamic motions upon reconstitution into POPC bilayers and the difference is in the cytosolic segment of PLB. 15N NMR studies of PLB on oriented membranes also indicated that the transmembrane segment of PLB aligns close to the bilayer normal, whereas the cytosolic segment aligns nearly perpendicular to the bilayer normal and closer to the membrane surface.
590 $a School code: 0126.
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0486
710 2 $a Miami University. $3 1017534
773 0 $t Dissertation Abstracts International $g 68-05B.
790 $a 0126
790 1 0 $a Lorigan, Gary A., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3264645