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NMR investigations of blood coagulat...

Boettcher, John Micheal.

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NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation./
Author:	Boettcher, John Micheal.
Description:	175 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: 7403.
Contained By:	Dissertation Abstracts International71-12B.
Subject:	Chemistry, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3430932
ISBN:	9781124323169

NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation.
Boettcher, John Micheal.

NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation. - 175 p.

Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: 7403.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010.

A multitude of biological processes involve membranes and their associated membrane proteins. The interactions of these biological molecules lead to perturbations in their structure and dynamics. Understanding the variations in the constitution of these molecules as the result of functional interactions will provide insights into various biological processes. In this work, we employ solution and solid-state NMR to observe changes in dynamics and conformation of both membranes and membrane associated proteins upon interaction with other biological molecules. Initial studies focus on the interaction of neurological proteins alpha-synuclein and endosulfinealpha. Using chemical shift perturbation mapping we detail interactions of membrane bound alpha-synuclein with cAMP-regulated phosphoproteins, ARPP-19 and endosulfine-alpha. Additionally, we report that endosulfine-alpha is an intrinsically unstructured protein that undergoes a conformational change upon binding to membranes and detail the effects of phosphorylation on these structures. Furthermore, using a combination of solution and solid-state NMR, we investigate important interactions involved in blood coagulation. Structural and dynamics data of Ca2+-induced clusters of phosphatidylserine in membranes, important in blood clotting, is investigated using isotopically 13C, 15N-labeled phosphatidylserine in lipid bilayers. Finally, backbone resonances of the soluble, extracellular domain of tissue factor (absent the membrane binding transmembrane helix) are assigned in solution and nanocrystalline samples by solution and solid-state NMR respectively. The chemical shifts are then used to investigate changes in the extracellular domain of tissue factor when bound to the membrane by its native transmembrane helix.

ISBN: 9781124323169Subjects--Topical Terms:

1021807
Chemistry, General.

NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation.
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020 $a 9781124323169
035 $a (UMI)AAI3430932
035 $a AAI3430932
040 $a UMI $c UMI
100 1 $a Boettcher, John Micheal. $3 1683943
245 1 0 $a NMR investigations of blood coagulation: Conformational changes of membrane bilayers and proteins in blood coagulation.
300 $a 175 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-12, Section: B, page: 7403.
500 $a Adviser: Chad M. Rienstra.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010.
520 $a A multitude of biological processes involve membranes and their associated membrane proteins. The interactions of these biological molecules lead to perturbations in their structure and dynamics. Understanding the variations in the constitution of these molecules as the result of functional interactions will provide insights into various biological processes. In this work, we employ solution and solid-state NMR to observe changes in dynamics and conformation of both membranes and membrane associated proteins upon interaction with other biological molecules. Initial studies focus on the interaction of neurological proteins alpha-synuclein and endosulfinealpha. Using chemical shift perturbation mapping we detail interactions of membrane bound alpha-synuclein with cAMP-regulated phosphoproteins, ARPP-19 and endosulfine-alpha. Additionally, we report that endosulfine-alpha is an intrinsically unstructured protein that undergoes a conformational change upon binding to membranes and detail the effects of phosphorylation on these structures. Furthermore, using a combination of solution and solid-state NMR, we investigate important interactions involved in blood coagulation. Structural and dynamics data of Ca2+-induced clusters of phosphatidylserine in membranes, important in blood clotting, is investigated using isotopically 13C, 15N-labeled phosphatidylserine in lipid bilayers. Finally, backbone resonances of the soluble, extracellular domain of tissue factor (absent the membrane binding transmembrane helix) are assigned in solution and nanocrystalline samples by solution and solid-state NMR respectively. The chemical shifts are then used to investigate changes in the extracellular domain of tissue factor when bound to the membrane by its native transmembrane helix.
590 $a School code: 0090.
650 4 $a Chemistry, General. $3 1021807
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0485
690 $a 0487
710 2 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 71-12B.
790 1 0 $a Rienstra, Chad M., $e advisor
790 $a 0090
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3430932