Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes.
Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes.
复制标题
渗透液诱导的水合水域之间氢键的扰动：与蛋白质构象变化的相关性。
DOI：
10.1021/jp9072284
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发表时间：
2009-12-31
期刊：
影响因子：
--
通讯作者：
Friedman JM
中科院分区：
文献类型：
--
作者：
Guo F;Friedman JM
钆振动边带发光光谱（GVSBLS）是用来探测渗透液引起的变化之间的氢键强度的第一和第二壳沃茨表面上的游离Gd 3+和Gd 3+协调EDTA和结构化的钙结合肽在溶液中。并行地，拉曼用于探测相同组的渗透剂对体相中的沃茨之间的氢键的相应影响。观察到添加的尿素的浓度增加逐渐削弱水合层内的氢键，但对本体水的影响最小。相比之下，观察到多元醇增强水合层和本体中的氢键合，其中幅度是多元醇依赖性的，海藻糖比蔗糖、葡萄糖或甘油更有效。所观察到的图案表明，渗透剂的大小和性质，以及水化的特定表面部位的局部结构影响优先排斥效应和局部氢键强度。作为添加的渗透剂的函数的肽的振动光谱与CD测量的相关性示出了与添加的多元醇的二级结构的增加，并且在添加尿素后氢键的逐渐减弱首先增加肽内的水占有率，并且仅随后肽展开。结果支持模型中，在展开过程中的初始步骤涉及渗透剂诱导的蛋白质内部的水占用的增强。
Gadolinium vibronic side band luminescent spectroscopy (GVSBLS) is used to probe osmolyte-induced changes in the hydrogen bond strength between first and second shell waters on the surface of free Gd3+ and Gd3+ coordinated to EDTA and to structured calcium binding peptides in solution. In parallel, Raman is used to probe the corresponding impact of the same set of osmolytes on hydrogen bonding among waters in the bulk phase. Increasing concentration of added urea is observed to progressively weaken the hydrogen bonding within the hydration layer but has minimal observed impact on bulk water. In contrast polyols are observed to enhance hydrogen bonding in both the hydration layer and the bulk with the amplitude being polyol dependent with trehalose being more effective than sucrose, glucose or glycerol. The observed patterns indicate that size and properties of the osmolyte as well as the local architecture of the specific surface site of hydration impacts preferential exclusion effects and local hydrogen bond strength. Correlation of the vibronic spectra with CD measurements on the peptides as a function of added osmolytes shows an increase in secondary structure with added polyols and that the progressive weakening of the hydrogen bonding upon addition of urea first increases water occupancy within the peptide and only subsequently does the peptide unfold. The results support models in which the initial steps in the unfolding process involves osmolyte induced enhancement of water occupancy within the interior of the protein.
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影响因子：
2.9
作者：
CHEN, YH;YANG, JT;MARTINEZ, HM
通讯作者：
MARTINEZ, HM
影响因子：
3.3
作者：
Dashnau, Jennifer L.;Nucci, Nathaniel V.;Vanderkooi, Jane M.
通讯作者：
Vanderkooi, Jane M.
影响因子：
3.3
作者：
Dashnau, JL;Sharp, KA;Vanderkooi, JM
通讯作者：
Vanderkooi, JM
影响因子：
4.4
作者：
Bellm, SM;Lawrance, WD
通讯作者：
Lawrance, WD
影响因子：
56.9
作者：
FRAUENFELDER, H;SLIGAR, SG;WOLYNES, PG
通讯作者：
WOLYNES, PG