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Studies of the structure and interac...

Gao, Xinfeng.

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Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation./
Author:	Gao, Xinfeng.
Description:	209 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2948.
Contained By:	Dissertation Abstracts International65-06B.
Subject:	Chemistry, Physical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3137700
ISBN:	0496848712

Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation.
Gao, Xinfeng.

Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation. - 209 p.

Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2948.

Thesis (Ph.D.)--University of Missouri - Columbia, 2004.

Several neuropeptides, adrenocorticotropin hormone (1--24), (1--10), and (11--24), Substance P [Tyr8], and Neurokinin A [Tyr 0], were studied by nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations in explicit (all-atom) membrane mimetic environments. The partition of these peptides in sodium dodecylsulfate (SDS) and dodecylphosphocholine (DPC) micelles, which are the most widely used "membrane mimics", was measured by NMR pulsed-field-gradient diffusion techniques. The "membrane-bound" conformation of these peptides was determined by two-dimensional NMR. The mode of binding (the location and orientation of the peptides with respect to the membrane/water interface) was investigated by the combined use of NMR and MD. The use of NMR diffusion techniques to study peptide binding, to measure thermodynamic functions, and the use of intermolecular nuclear Overhauser effect between peptide and micelle are all new approaches in studying peptide-membrane interactions. The MD simulation results were correlated to the NMR experimental data, rendering a picture of peptide/membrane interaction at atomic level. The current results were also compared with the results of the same peptides in lipid bilayers.

ISBN: 0496848712Subjects--Topical Terms:

560527
Chemistry, Physical.

Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation.
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245 1 0 $a Studies of the structure and interaction of several neuropeptides in membrane mimics by NMR spectroscopy and molecular dynamics simulation.
300 $a 209 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2948.
500 $a Supervisor: Tuck C. Wong.
502 $a Thesis (Ph.D.)--University of Missouri - Columbia, 2004.
520 $a Several neuropeptides, adrenocorticotropin hormone (1--24), (1--10), and (11--24), Substance P [Tyr8], and Neurokinin A [Tyr 0], were studied by nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations in explicit (all-atom) membrane mimetic environments. The partition of these peptides in sodium dodecylsulfate (SDS) and dodecylphosphocholine (DPC) micelles, which are the most widely used "membrane mimics", was measured by NMR pulsed-field-gradient diffusion techniques. The "membrane-bound" conformation of these peptides was determined by two-dimensional NMR. The mode of binding (the location and orientation of the peptides with respect to the membrane/water interface) was investigated by the combined use of NMR and MD. The use of NMR diffusion techniques to study peptide binding, to measure thermodynamic functions, and the use of intermolecular nuclear Overhauser effect between peptide and micelle are all new approaches in studying peptide-membrane interactions. The MD simulation results were correlated to the NMR experimental data, rendering a picture of peptide/membrane interaction at atomic level. The current results were also compared with the results of the same peptides in lipid bilayers.
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650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
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710 2 0 $a University of Missouri - Columbia. $3 1017522
773 0 $t Dissertation Abstracts International $g 65-06B.
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