Unfolding of α-helical 20-residue poly-glutamic acid analyzed by multiple runs of canonical molecular dynamics simulations.

导出 LinkOut

翻译打印收藏纠错

作者： Naoki,Ogasawara ^[1] ; Kota,Kasahara ^[2] ; Ryosuke,Iwai ^[1] ; Takuya,Takahashi ^[2]

作者单位： Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan. ^[1] College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan. ^[2]

关键词 Conformational change Disorder Helix unfolding Helix–coil equilibrium Helix–coil transition Molecular dynamics Molecular simulation Peptide denaturation Poly-glutamic acid Polypeptide

DOI 10.7717/peerj.4769

PMID 29780670

发布时间 2020-10-01

翻译满意度评价：

准确一般字义偏差语意偏离译文作用小提交

浏览12

PeerJ

2018年6卷

e4769页

相似文献

中文期刊
外文期刊
学位论文
会议论文

检索历史清除

Unfolding of α-helical 20-residue poly-glutamic acid analyzed by multiple runs of canonical molecular dynamics simulations.

PeerJ

相似文献

PeerJ

相关期刊

参考文献：
指定格式：	NoteExpress EndNote RefWorks NoteFirst

检索历史 清除

Unfolding of α-helical 20-residue poly-glutamic acid analyzed by multiple runs of canonical molecular dynamics simulations.

PeerJ

相似文献

PeerJ

相关期刊

检索历史清除