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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| Format: | Others |
| Language: | zh-TW |
| Published: |
2008
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| Online Access: | http://ndltd.ncl.edu.tw/handle/55498985094256966249 |
| Summary: | 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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