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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Interactions of proteins in aqueous electrolyte solutions from fluorescence anisotropy and circular-dichroism measurements.
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Interactions of proteins in aqueous electrolyte solutions from fluorescence anisotropy and circular-dichroism measurements.

机译：通过荧光各向异性和圆二色性测量，电解质水溶液中蛋白质的相互作用。

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摘要

Understanding aqueous protein-protein interactions is crucial for the development of a molecular-thermodynamic model for salt-induced protein precipitation. In addition, protein interactions are important in many disease states, including cataract formation and alpha-amyloid diseases. Fluorescence anisotropy provides a means to measure intermolecular interactions. In this work, monomer-dimer equilibrium of the peptide T4 LYS(11-36) was studied by fluorescence anisotropy over the pH range 4-7 and the NaCl concentration range 0.0-1.0 M, in a 25 mM sodium phosphate buffer. This 26 amino-acid peptide is derived from the beta-sheet region of the T4 lysozyme molecule and has the potential to form amyloid fibrils. The association constant for dimerization increases with rising pH and ionic strength. The potential of mean force for peptide-peptide interactions was calculated from these association constants. Circular-dichroism measurements show that the peptide becomes more structured as the pH rises, possibly contributing to increased association.
机译：了解水-蛋白质相互作用对盐诱导的蛋白质沉淀的分子热力学模型的开发至关重要。另外，蛋白质相互作用在许多疾病状态中也很重要，包括白内障形成和α-淀粉样蛋白疾病。荧光各向异性提供了一种测量分子间相互作用的方法。在这项工作中，在25 mM磷酸钠缓冲液中，通过在pH范围4-7和NaCl浓度范围0.0-1.0 M范围内的荧光各向异性研究了肽T4 LYS（11-36）的单体-二聚体平衡。该26个氨基酸的肽衍生自T4溶菌酶分子的β-折叠区域，具有形成淀粉样蛋白原纤维的潜力。随着pH值和离子强度的提高，二聚化的缔合常数增加。从这些缔合常数计算肽-肽相互作用的平均力的潜力。圆二色性测量表明，随着pH的升高，肽变得更加结构化，可能有助于缔合。

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