D-Proline effects on Peptidyl-prolyl cis/trans Isomerization
碩士 === 輔仁大學 === 化學系 === 96 === Amino acids are the basic structural units of proteins. The nature of amino acids can influence the structural and the function of the protein. Proline residues have often been associated with conformational changes in peptides and proteins, because of their unique abi...
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ndltd-TW-096FJU000650232015-10-13T13:47:38Z http://ndltd.ncl.edu.tw/handle/55498985094256966249 D-Proline effects on Peptidyl-prolyl cis/trans Isomerization D-脯胺酸Peptidyl-prolylcis/trans異構化的影響 Tsu-Pin Wang 王祖濱 碩士 輔仁大學 化學系 96 Amino acids are the basic structural units of proteins. The nature of amino acids can influence the structural and the function of the protein. Proline residues have often been associated with conformational changes in peptides and proteins, because of their unique ability to undergo peptidyl-prolyl cis/trans isomerization about peptide bond linking proline and preceding amino acid residue. In order to examine the ability of L-amino acid residues preceding D-proline, Xaa-D-Pro, to stabilize a cis amide conformation relative to that observed with L-proline, we prepare a series of D-proline analogs of linear peptides that contain an amide bond between L-amino acid and D-proline. The D-proline containing peptides were prepared with the soild-phase peptide synthesis procols. Conformation studies on the peptidyl-prolyl cis/trans isomerization of D-proline peptides were analyzed by 1H NMR. Heau-Shan Gao 高華生 2008 學位論文 ; thesis 194 zh-TW |
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碩士 === 輔仁大學 === 化學系 === 96 === Amino acids are the basic structural units of proteins. The nature of amino acids can influence the structural and the function of the protein. Proline residues have often been associated with conformational changes in peptides and proteins, because of their unique ability to undergo peptidyl-prolyl cis/trans isomerization about peptide bond linking proline and preceding amino acid residue. In order to examine the ability of L-amino acid residues preceding D-proline, Xaa-D-Pro, to stabilize a cis amide conformation relative to that observed with L-proline, we prepare a series of D-proline analogs of linear peptides that contain an amide bond between L-amino acid and D-proline. The D-proline containing peptides were prepared with the soild-phase peptide synthesis procols. Conformation studies on the peptidyl-prolyl cis/trans isomerization of D-proline peptides were analyzed by 1H NMR.
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author2 |
Heau-Shan Gao |
author_facet |
Heau-Shan Gao Tsu-Pin Wang 王祖濱 |
author |
Tsu-Pin Wang 王祖濱 |
spellingShingle |
Tsu-Pin Wang 王祖濱 D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
author_sort |
Tsu-Pin Wang |
title |
D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
title_short |
D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
title_full |
D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
title_fullStr |
D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
title_full_unstemmed |
D-Proline effects on Peptidyl-prolyl cis/trans Isomerization |
title_sort |
d-proline effects on peptidyl-prolyl cis/trans isomerization |
publishDate |
2008 |
url |
http://ndltd.ncl.edu.tw/handle/55498985094256966249 |
work_keys_str_mv |
AT tsupinwang dprolineeffectsonpeptidylprolylcistransisomerization AT wángzǔbīn dprolineeffectsonpeptidylprolylcistransisomerization AT tsupinwang dpúànsuānpeptidylprolylcistransyìgòuhuàdeyǐngxiǎng AT wángzǔbīn dpúànsuānpeptidylprolylcistransyìgòuhuàdeyǐngxiǎng |
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1717741547477270528 |