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Orientation and NMR for membrane pro...

Mesleh, Michael Farah.

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Orientation and NMR for membrane protein structure determination.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Orientation and NMR for membrane protein structure determination./
Author:	Mesleh, Michael Farah.
Description:	196 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1849.
Contained By:	Dissertation Abstracts International65-04B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3129935
ISBN:	0496771906

Orientation and NMR for membrane protein structure determination.
Mesleh, Michael Farah.

Orientation and NMR for membrane protein structure determination. - 196 p.

Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1849.

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

Membrane proteins represent one of the great challenges of modern structural biology. In the absence of suitable samples for standard methods of X-Ray Crystallography and NMR Spectroscopy, methods tailored to the extraction of maximum structure information from minimum experimental data have emerged from a wide variety of sources. New methods for the alignment of proteins by solution-state NMR spectroscopy have paralleled the development of solid-state NMR methods in such a way that the tools for structure determination could be applied similarly in both cases. Methods presented in this Thesis show that the high-resolution structural information inherent to dipolar couplings measured from aligned samples of membrane proteins are sufficient to determine high-resolution protein structures. Using the basic properties of anisotropic NMR observables such as chemical shifts and dipolar couplings, it is shown that the periodic properties of alpha-helices allow for the extraction of secondary structural information, as well as information about the orientations and deviations from ideality of individual helices in proteins. This information can then be used to build models of proteins of high quality using preexisting structure calculation methods. Methods are then applied to several examples of membrane proteins, enabling comparisons to be made between the environments of micelles and those of lipid bilayers. Finally, the methods developed in this Thesis are applied to the bacterial Hg+2 transporter MerF, a two-transmembrane helix protein in lipid micelles.

ISBN: 0496771906Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Orientation and NMR for membrane protein structure determination.
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100 1 $a Mesleh, Michael Farah. $3 1935769
245 1 0 $a Orientation and NMR for membrane protein structure determination.
300 $a 196 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1849.
500 $a Chair: Stanley J. Opella.
502 $a Thesis (Ph.D.)--University of California, San Diego, 2004.
520 $a Membrane proteins represent one of the great challenges of modern structural biology. In the absence of suitable samples for standard methods of X-Ray Crystallography and NMR Spectroscopy, methods tailored to the extraction of maximum structure information from minimum experimental data have emerged from a wide variety of sources. New methods for the alignment of proteins by solution-state NMR spectroscopy have paralleled the development of solid-state NMR methods in such a way that the tools for structure determination could be applied similarly in both cases. Methods presented in this Thesis show that the high-resolution structural information inherent to dipolar couplings measured from aligned samples of membrane proteins are sufficient to determine high-resolution protein structures. Using the basic properties of anisotropic NMR observables such as chemical shifts and dipolar couplings, it is shown that the periodic properties of alpha-helices allow for the extraction of secondary structural information, as well as information about the orientations and deviations from ideality of individual helices in proteins. This information can then be used to build models of proteins of high quality using preexisting structure calculation methods. Methods are then applied to several examples of membrane proteins, enabling comparisons to be made between the environments of micelles and those of lipid bilayers. Finally, the methods developed in this Thesis are applied to the bacterial Hg+2 transporter MerF, a two-transmembrane helix protein in lipid micelles.
590 $a School code: 0033.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Biology, Cell. $3 1017686
690 $a 0487
690 $a 0786
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710 2 0 $a University of California, San Diego. $3 1018093
773 0 $t Dissertation Abstracts International $g 65-04B.
790 1 0 $a Opella, Stanley J., $e advisor
790 $a 0033
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3129935