The orientation and dynamics of somatostatin in lipid environment

碩士 === 朝陽科技大學 === 應用化學系碩士班 === 91 === In this article, NMR methods are applied to explore the orientation and dynamics of somatostatin at lipid surface. The presence of sodium dodecylsulfate (SDS) micelles has been found to cause sequence specific changes in the acid- and base-catalyzed amide proton...

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Main Authors: Yi-Cheng Cheng, 陳亦徵
Other Authors: none
Format: Others
Language:zh-TW
Published: 2003
Online Access:http://ndltd.ncl.edu.tw/handle/d3k526
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spelling ndltd-TW-091CYUT55000182018-06-25T06:06:27Z http://ndltd.ncl.edu.tw/handle/d3k526 The orientation and dynamics of somatostatin in lipid environment 體制素在脂質環境中的位置及動力學性質 Yi-Cheng Cheng 陳亦徵 碩士 朝陽科技大學 應用化學系碩士班 91 In this article, NMR methods are applied to explore the orientation and dynamics of somatostatin at lipid surface. The presence of sodium dodecylsulfate (SDS) micelles has been found to cause sequence specific changes in the acid- and base-catalyzed amide proton exchange rates relative to the solution state values. On binding of somatostatin to SDS micelles, the FFWKT segment showed the most obvious decrease in the base-catalyzed amide exchange rates. The sequence-specific effects of micelle association were also observed in the homonuclear nonselective spin-lattice relaxation time (T1). These data combined with paramagnetic broadening observation on peptide protons in the presence of spin-labeled lipids yield a detailed model of the interaction of somatostatin with lipid surface. The association of somatostatin to the SDS micelle is further determined by pulsed-field-gradient NMR technique. The association constant is 1.03×103 M-1. This association is thus proved to be a spontaneous process. none 錢偉鈞 2003 學位論文 ; thesis 127 zh-TW
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language zh-TW
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description 碩士 === 朝陽科技大學 === 應用化學系碩士班 === 91 === In this article, NMR methods are applied to explore the orientation and dynamics of somatostatin at lipid surface. The presence of sodium dodecylsulfate (SDS) micelles has been found to cause sequence specific changes in the acid- and base-catalyzed amide proton exchange rates relative to the solution state values. On binding of somatostatin to SDS micelles, the FFWKT segment showed the most obvious decrease in the base-catalyzed amide exchange rates. The sequence-specific effects of micelle association were also observed in the homonuclear nonselective spin-lattice relaxation time (T1). These data combined with paramagnetic broadening observation on peptide protons in the presence of spin-labeled lipids yield a detailed model of the interaction of somatostatin with lipid surface. The association of somatostatin to the SDS micelle is further determined by pulsed-field-gradient NMR technique. The association constant is 1.03×103 M-1. This association is thus proved to be a spontaneous process.
author2 none
author_facet none
Yi-Cheng Cheng
陳亦徵
author Yi-Cheng Cheng
陳亦徵
spellingShingle Yi-Cheng Cheng
陳亦徵
The orientation and dynamics of somatostatin in lipid environment
author_sort Yi-Cheng Cheng
title The orientation and dynamics of somatostatin in lipid environment
title_short The orientation and dynamics of somatostatin in lipid environment
title_full The orientation and dynamics of somatostatin in lipid environment
title_fullStr The orientation and dynamics of somatostatin in lipid environment
title_full_unstemmed The orientation and dynamics of somatostatin in lipid environment
title_sort orientation and dynamics of somatostatin in lipid environment
publishDate 2003
url http://ndltd.ncl.edu.tw/handle/d3k526
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