Searching for folding initiation sites of staphylococcal nuclease: A study of N‐terminal short fragments
Searching for folding initiation sites of staphylococcal nuclease: A study of N‐terminal short fragments
复制标题
寻找葡萄球菌核酸酶的折叠起始位点：N 端短片段的研究
DOI：
10.1002/bip.20121
复制
发表时间：
2004
期刊：
影响因子：
2.9
通讯作者：
Jinfeng Wang
中科院分区：
文献类型：
--
作者：
J. Dai;Xu Wang;Yingang Feng;G. Fan;Jinfeng Wang
已合成了葡萄球菌核酸酶（SNase）的N末端短片段SNase 20、SNase 28和SNase 36，分别对应于序列区域Ala 1-Gly 20、Ala 1-Lys 28和Ala 1-Leu 36，以及8残基肽（Ala 17-Ile 18-Asp 19-Gly 20-Asp 21-Thr 22-Val 23-Lys 24）。利用CD和NMR光谱研究了这些片段在水溶液和三氟乙醇（TFE）-H2O混合物中的构象状态。含有与天然SNase中的弯曲肽相对应的序列的SNase 20在TFE-H2O混合物中显示围绕Ala 12-Thr 13-Leu 14的弯曲样构象的瞬时群体。SNase 28的Ala 17-Thr 22序列区在水溶液和TFE-H2O混合物中均显示出转向样构象的局部倾向。SNase 36在水溶液中的构象系综包括位于序列区Ala 17-Thr 22和Tyr 27-Gln 30中的聚集的转弯样构象。分析表明，这些形成天然蛋白质中规则二级结构的序列区域可以作为从N末端开始的不同链长的SNase片段的折叠成核位点。因此，这些序列区域的弯曲和转弯样构象的形成可能参与SNase多肽链在体外的早期折叠事件。© 2004 Wiley Periodicals，Inc.生物聚合物，2004年
The N‐terminal short fragments of staphylococcal nuclease (SNase), SNase20, SNase28, and SNase36, corresponding to the sequence regions, Ala1–Gly20, Ala1–Lys28, and Ala1–Leu36, respectively, as well as an 8‐residue peptide (Ala17–Ile18–Asp19–Gly20–Asp21–Thr22–Val23–Lys24) have been synthesized. The conformational states of these fragments were investigated using CD and NMR spectroscopy in aqueous solution and in trifluoroethanol (TFE)–H2O mixture. SNase20 containing a sequence corresponding to a bent peptide in native SNase shows a transient population of bend‐like conformation around Ala12–Thr13–Leu14 in TFE–H2O mixture. The sequence region of Ala17–Thr22 of SNase28 displays a localized propensity for turn‐like conformation in both aqueous solution and TFE—H2O mixture. The conformational ensemble of SNase36 in aqueous solution includes populated turn‐like conformations localized in sequence regions Ala17–Thr22 and Tyr27–Gln30. The analysis suggests that these sequence regions, which form the regular secondary structures in native protein, may serve as the folding nucleation sites of SNase fragments of different chain lengths starting from the N‐terminal end. Thus, the formation of bend‐ and turn‐like conformations of these sequence regions may be involved in the early folding events of the SNase polypeptide chain in vitro. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004
登录
查看更多内容
DOI：
10.1146/annurev.bb.20.060191.002511
发表时间：
1991
期刊：
Annual review of biophysics and biophysical chemistry
影响因子：
--
作者：
Dyson Hj;P. Wright
通讯作者：
Dyson Hj;P. Wright
水溶液中蛋白质肽片段的构象：对蛋白质折叠起始的影响。
影响因子：
2.9
作者：
Wright,PE;Dyson,HJ;Lerner,RA
通讯作者：
Lerner,RA
影响因子：
5.6
作者：
DYSON, HJ;RANCE, M;WRIGHT, PE
通讯作者：
WRIGHT, PE
影响因子：
2.9
作者：
W. F. Walkenhorst;S. Green;H. Roder
通讯作者：
W. F. Walkenhorst;S. Green;H. Roder
蛋白质折叠起始位点的肽模型。
影响因子：
2.9
作者：
Shin,HC;Merutka,G;Waltho,JP;Wright,PE;Dyson,HJ
通讯作者：
Dyson,HJ