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学科主题: 基础医学
题名:
de novo Design and conformational studies of a beta-hairpin forming peptide
作者: Sha, YL1; Li, YL1; Qiu, Y1; Wang, Q1; Lai, LH1
关键词: de novo design ; beta-hairpin ; beta-turn ; beta-sheet ; cross-strand amino acid pairs ; CD ; FTIR
刊名: ACTA PHYSICO-CHIMICA SINICA
发表日期: 2002-10-01
DOI: 10.3866/PKU.WHXB20021008
卷: 18, 期:10, 页:907-910
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Chemistry, Physical
研究领域[WOS]: Chemistry
关键词[WOS]: QUANTITATIVE IR SPECTROPHOTOMETRY ; WATER H2O SOLUTIONS ; SECONDARY STRUCTURE ; CIRCULAR-DICHROISM ; ABSORPTION-BANDS ; PROTEIN ; SPECTROSCOPY ; NMR ; FRAGMENT ; POLYPEPTIDES
英文摘要:

A 12-residue peptide (R(1)G(2)T(3)F(4)W(5)V(6)d-(PSVNYF12)-S-7-V-8-N-9-Y-10-F-11, beta2) with cross-strand amino acid pairs (VV9)-V-6, (FY11)-Y-4 and (YF12)-F-3, predicted to form beta-hairpin, was designed and synthesized by Fmoc/Bu′strategy. The circular dichroism spectrum of beta2 in PBS buffer shows a maximum at about 202 run and a minimum at about 217. 5 nm, a typical beta-hairpin characteristics that have been postulated as the common contribution from a beta-turn. mixed with a beta-sheet. The FTIR experiments confirmed the secondary structural contents of beta2.

语种: 中文
WOS记录号: WOS:000178709800009
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/51650
Appears in Collections:基础医学院_生物物理学系_期刊论文

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作者单位: 1.Peking Univ, Inst Chem Phys, Beijing 100871, Peoples R China
2.Peking Univ, Sch Basic Med Sci, Dept Biophys, Single Mol & Nanobiomed Lab, Beijing 100083, Peoples R China

Recommended Citation:
Sha, YL,Li, YL,Qiu, Y,et al. de novo Design and conformational studies of a beta-hairpin forming peptide[J]. ACTA PHYSICO-CHIMICA SINICA,2002,18(10):907-910.
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