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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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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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.
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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 |
work_keys_str_mv |
AT yichengcheng theorientationanddynamicsofsomatostatininlipidenvironment AT chényìzhēng theorientationanddynamicsofsomatostatininlipidenvironment AT yichengcheng tǐzhìsùzàizhīzhìhuánjìngzhōngdewèizhìjídònglìxuéxìngzhì AT chényìzhēng tǐzhìsùzàizhīzhìhuánjìngzhōngdewèizhìjídònglìxuéxìngzhì AT yichengcheng orientationanddynamicsofsomatostatininlipidenvironment AT chényìzhēng orientationanddynamicsofsomatostatininlipidenvironment |
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1718706196474494976 |