Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach
碩士 === 國立清華大學 === 生物資訊與結構生物研究所 === 92 === Cobra phospholipase A2, a α-helix acidic polypeptide, is known to hydrolyze membrane and involve some cell signaling pathways. Herein, we demonstrate that the major cobra phospholipase A2 ( Naja atra ), By the combined polarized attenuated total reflection i...
Main Author: | |
---|---|
Other Authors: | |
Format: | Others |
Language: | zh-TW |
Published: |
2004
|
Online Access: | http://ndltd.ncl.edu.tw/handle/at3zdz |
id |
ndltd-TW-092NTHU5112012 |
---|---|
record_format |
oai_dc |
spelling |
ndltd-TW-092NTHU51120122019-05-15T19:38:04Z http://ndltd.ncl.edu.tw/handle/at3zdz Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach 結合傅氏紅外線光譜儀及電腦模擬計算研究眼鏡蛇磷脂水解酵素A2與細胞膜之間的作用 謝怡慧 碩士 國立清華大學 生物資訊與結構生物研究所 92 Cobra phospholipase A2, a α-helix acidic polypeptide, is known to hydrolyze membrane and involve some cell signaling pathways. Herein, we demonstrate that the major cobra phospholipase A2 ( Naja atra ), By the combined polarized attenuated total reflection infrared spectroscopy and computer simulation studies, Naja atra phospholipase A2 is shown to peripherally bind to multilayers in a similar edgewise manner with a tilted angle of 160° between theα-helix plane of the Cobra phospholipase A2 molecule and the normal of the membrane surface. Qualitatively speaking, theα-helix plane of the Cobra phospholipase A2 molecule with (90°,60°) orientation appears to be more perpendicular to the membrane surface than that with (160°, 60°) orientation. 吳文桂 2004 學位論文 ; thesis 66 zh-TW |
collection |
NDLTD |
language |
zh-TW |
format |
Others
|
sources |
NDLTD |
description |
碩士 === 國立清華大學 === 生物資訊與結構生物研究所 === 92 === Cobra phospholipase A2, a α-helix acidic polypeptide, is known to hydrolyze membrane and involve some cell signaling pathways. Herein, we demonstrate that the major cobra phospholipase A2 ( Naja atra ), By the combined polarized attenuated total reflection infrared spectroscopy and computer simulation studies, Naja atra phospholipase A2 is shown to peripherally bind to multilayers in a similar edgewise manner with a tilted angle of 160° between theα-helix plane of the Cobra phospholipase A2 molecule and the normal of the membrane surface.
Qualitatively speaking, theα-helix plane of the Cobra phospholipase A2 molecule with (90°,60°) orientation appears to be more perpendicular to the membrane surface than that with (160°, 60°) orientation.
|
author2 |
吳文桂 |
author_facet |
吳文桂 謝怡慧 |
author |
謝怡慧 |
spellingShingle |
謝怡慧 Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
author_sort |
謝怡慧 |
title |
Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
title_short |
Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
title_full |
Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
title_fullStr |
Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
title_full_unstemmed |
Peripheral binding mode of cobra phospholipase A2 on phospholipid membranes as studied by combined FTIR and computer simulation approach |
title_sort |
peripheral binding mode of cobra phospholipase a2 on phospholipid membranes as studied by combined ftir and computer simulation approach |
publishDate |
2004 |
url |
http://ndltd.ncl.edu.tw/handle/at3zdz |
work_keys_str_mv |
AT xièyíhuì peripheralbindingmodeofcobraphospholipasea2onphospholipidmembranesasstudiedbycombinedftirandcomputersimulationapproach AT xièyíhuì jiéhéfùshìhóngwàixiànguāngpǔyíjídiànnǎomónǐjìsuànyánjiūyǎnjìngshélínzhīshuǐjiějiàosùa2yǔxìbāomózhījiāndezuòyòng |
_version_ |
1719092104000438272 |