Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides.

Hydration and conformational mechanics of single, end-tethered elastin-like polypeptides.
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DOI:
10.1021/ja800502h
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发表时间:
2008-08-20
影响因子:
15
通讯作者:
Zauscher S
Zauscher S
中科院分区:
化学1区
文献类型:
--
作者:
Valiaev A;Lim DW;Schmidler S;Clark RL;Chilkoti A;Zauscher S

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我们使用单分子力谱 (SMFS) 研究了温度、离子强度、溶剂极性和客体残基类型对单个末端束缚弹性蛋白样多肽 (ELP) 的力延伸行为的影响。 ELP 是刺激响应性多肽,包含五个氨基酸 Val-Pro-Gly-Xaa-Gly (VPGXG) 的重复序列,其中 Xaa 是客体残基,可以是除脯氨酸外的任何氨基酸。我们将力延伸数据与自由连接链 (FJC) 模型进行拟合,该模型使我们能够解决有效库恩段长度分布的微小差异,这些差异主要是由 ELP 的疏水水合行为的差异引起的。我们的结果与最近分子动力学模拟的预测定性一致,并证明疏水水合调节 ELP 的分子弹性。此外,我们的结果表明,当与我们的数据分析方法相结合时,SMFS 可用于研究多肽-水相互作用的微妙之处,从而为本质上非结构化生物大分子中疏水水合的研究提供基础。
We investigated the effect of temperature, ionic strength, solvent polarity, and type of guest residue on the force—extension behavior of single, end-tethered elastin-like polypeptides (ELPs), using single molecule force spectroscopy (SMFS). ELPs are stimulus-responsive polypeptides that contain repeats of the five amino acids Val-Pro-Gly-Xaa-Gly (VPGXG), where Xaa is a guest residue that can be any amino acid with the exception of proline. We fitted the force—extension data with a freely jointed chain (FJC) model which allowed us to resolve small differences in the effective Kuhn segment length distributions that largely arise from differences in the hydrophobic hydration behavior of ELP. Our results agree qualitatively with predictions from recent molecular dynamics simulations and demonstrate that hydrophobic hydration modulates the molecular elasticity for ELPs. Furthermore, our results show that SMFS, when combined with our approach for data analysis, can be used to study the subtleties of polypeptide—water interactions and thus provides a basis for the study of hydrophobic hydration in intrinsically unstructured biomacromolecules.
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