Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge-charge interactions.
Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge-charge interactions.
复制标题
L9 N 端结构域展开状态下的残余静电效应可归因于非特异性非局部电荷-电荷相互作用。
DOI：
10.1021/bi025580m
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发表时间：
2002
期刊：
影响因子：
2.9
通讯作者：
Zhou,Huan-Xiang
中科院分区：
文献类型：
--
作者：
Zhou,Huan-Xiang
Kuhlman 等人发现了 L9 (NTL9) N 端结构域展开状态下的残余静电相互作用。 [(1999)生物化学 38, 4896−4903]。这些残余相互作用在这里通过高斯链模型进行分析 [Zhou, H.-X. (2002)Proc。国家。阿卡德。科学。美国 99, 3569−3574]。通过用 Kuhlman 等人测量的值替换可电离基团的“标准”模型化合物 pKa 值，使原始模型更加真实。 NTL9 的肽片段。预测的展开自由能的 pH 依赖性与 pH 范围 1−7、离子强度 100 和 750 mM 的实验一致。这表明 NTL9 展开状态下的残余静电效应可归因于非特异性非局域电荷相互作用。
Residual electrostatic interactions in the unfolded state of the N-terminal domain of L9 (NTL9) were found by Kuhlman et al. [(1999)Biochemistry 38, 4896−4903]. These residual interactions are analyzed here by the Gaussian-chain model [Zhou, H.-X. (2002)Proc. Natl. Acad. Sci. U.S.A. 99, 3569−3574]. The original model is made more realistic by replacing “standard” model-compound pKavalues for ionizable groups by those measured by Kuhlman et al. in peptide fragments of NTL9. The predicted pH dependence of the unfolding free energy is in agreement with experiment over the pH range of 1−7 at ionic strengths of 100 and 750 mM. This indicates that the residual electrostatic effects in the unfolded state of NTL9 can be attributed to nonspecific nonlocal charge−charge interactions.