Hydrogen bonding of beta-turn structure is stabilized in D(2)O.
Hydrogen bonding of beta-turn structure is stabilized in D(2)O.
复制标题
DOI：
10.1021/ja9040785
复制
发表时间：
2009-10-28
影响因子：
15
通讯作者：
Cremer, Paul S.
中科院分区：
文献类型：
--
作者：
Cho, Younhee;Sagle, Laura B.;Iimura, Satoshi;Zhang, Yanjie;Kherb, Jaibir;Chilkoti, Ashutosh;Scholtz, J. Martin;Cremer, Paul S.
研究了弹性蛋白样多肽（ELP）的低临界溶解温度（LCST）与ELP链长和客体残基化学的关系。这些测量在D2 O和H2O中进行。与重水和轻水的LCST值的差异与多肽链的二级结构形成相关。这种结构信息是通过圆二色性和红外测量获得的。通过差示扫描量热法获得了额外的热力学数据。发现对于形成最大量的β-转角/β-聚集体结构的那些多肽，H_2O和D_2O之间的LCST值有较大的变化。此外，这些相同的分子是最不疏水的ELP。因此，氢键，而不是疏水性的ELP在D2 O中的塌陷状态的稳定性相比，水的关键因素。
The lower critical solution temperature (LCST) of elastin-like polypeptides (ELPs) was investigated as a function of ELP chain length and guest residue chemistry. These measurements were made in both D2O and H2O. Differences in the LCST values with heavy and light water were correlated with secondary structure formation of the polypeptide chains. Such structural information was obtained by circular dichroism and infrared measurements. Additional thermodynamic data were obtained by differential scanning calorimetry. It was found that there is a greater change in the LCST value between H2O and D2O for those polypeptides which form the greatest amount of β-turn/β-aggregate structure. Moreover, these same molecules were the least hydrophobic ELPs. Therefore, hydrogen bonding rather than hydrophobicity was the key factor in the stabilization of the collapsed state of ELPs in D2O compared with H2O.
登录
查看更多内容
影响因子：
2.9
作者：
Kumashiro, KK;Kurano, TL;Tamburro, AM
通讯作者：
Tamburro, AM
影响因子：
15
作者：
Mao, HB;Li, CM;Cremer, PS
通讯作者：
Cremer, PS
DOI：
10.1073/pnas.88.17.7715
发表时间：
1991-09-01
影响因子：
11.1
作者：
ANTONINO, LC;KAUTZ, RA;FINK, AL
通讯作者：
FINK, AL
DOI：
10.1038/nsb0696-522
发表时间：
1996-06-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Bowers, PM;Klevit, RE
通讯作者：
Klevit, RE
影响因子：
2.9
作者：
HATTORI, A;CRESPI, HL;KATZ, JJ
通讯作者：
KATZ, JJ