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Study of structure-function correlat...

Mo, Yiming.

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Study of structure-function correlations in ion channels by solid state NMR.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Study of structure-function correlations in ion channels by solid state NMR./
Author:	Mo, Yiming.
Description:	113 p.
Notes:	Adviser: Timothy A. Cross.
Contained By:	Dissertation Abstracts International67-04B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3216518
ISBN:	9780542660498

Study of structure-function correlations in ion channels by solid state NMR.
Mo, Yiming.

Study of structure-function correlations in ion channels by solid state NMR. - 113 p.

Adviser: Timothy A. Cross.

Thesis (Ph.D.)--The Florida State University, 2006.

Structural biology of membrane proteins and ion channels are of great interest because of their important roles in many cellular and physiological processes including ion/molecular transport, communication and energy transduction. Apart from x-ray crystallography, EPR, solution NMR, and electron diffraction, solid state NMR is an alternative method for the study of structural/functional correlations.

ISBN: 9780542660498Subjects--Topical Terms:

1019105
Biophysics, General.

Study of structure-function correlations in ion channels by solid state NMR.
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020 $a 9780542660498
035 $a (UMI)AAI3216518
035 $a AAI3216518
040 $a UMI $c UMI
100 1 $a Mo, Yiming. $3 1288186
245 1 0 $a Study of structure-function correlations in ion channels by solid state NMR.
300 $a 113 p.
500 $a Adviser: Timothy A. Cross.
500 $a Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1872.
502 $a Thesis (Ph.D.)--The Florida State University, 2006.
520 $a Structural biology of membrane proteins and ion channels are of great interest because of their important roles in many cellular and physiological processes including ion/molecular transport, communication and energy transduction. Apart from x-ray crystallography, EPR, solution NMR, and electron diffraction, solid state NMR is an alternative method for the study of structural/functional correlations.
520 $a Structures of many transmembrane domains (TMDs) of membrane proteins have been solved by solid state NMR. To apply that method to full length membrane protein, the conditions for oriented samples were optimized with M2 protein from Influenza A. 15N-Leu specific labeled M2 protein have been overexpressed in E. Coli, purified and reconstituted intolipid bilayers. Lipid bilayers were uniformly aligned on glass slides. The orientation of M2 protein was monitored by 15N-NMR. Several parameters were used in sample preparation: composition of lipid bilayers, hydration level, protein-lipid molar ratio, and detergents. The most important parameter is the detergent used in sample preparation. Samples prepared by using a strong detergent such as SDS resulted in 80% of the M2 protein being aligned while use of a weak detergent like OG resulted in only 40%. The NMR spectra also support a tilt angle of 20 +/- 5° for the transmembrane domain.
520 $a The ion interactions with KcsA, a potassium channel from Streptomyces lividans were studied by 87Rb NMR. KcsA was overexpressed in E. Coli, purified and reconstituted in DOPC/DOPG (4:1) liposomes. The 87Rb NMR study supported a two-step model for how ions enter the channel from bulk solution. The rubidium ions bind to the lipid bilayers first and then the lipid bound rubidium ions transfer to the protein's pore region of the channel. The rate of first step is slow but greater than 10 Hz. The second step is faster (>> 300 Hz). The binding constant of rubidium ions to KcsA was estimated to be 65 M-1 when [Rb +] = 2mM, by assuming a first order binding process. Such a mechanism suggests a novel way for Ca2+ to inhibit the channel function. Potentially, by depleting the surrounding lipid of Rb+ or K +, Ca2+ may inhibit conductance.
590 $a School code: 0071.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 0 $a The Florida State University. $3 1017727
773 0 $t Dissertation Abstracts International $g 67-04B.
790 $a 0071
790 1 0 $a Cross, Timothy A., $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3216518