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Thermodynamic characterizations of coulombic end effects and coupled folding effects on binding of cationic oligopeptides to nucleic acids. Two-domain of preferential solute-protein interactions.

机译:库仑末端效应和对阳离子寡肽与核酸结合的折叠效应的热力学表征。优先溶质-蛋白质相互作用的两个域。

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摘要

The research presented here addresses important questions about thermodynamic effects of salt-nucleic acid interactions on ligand-DNA binding and effects of solute-protein interactions on protein stability. Model systems are used to investigate the thermodynamic basis of two major coupled processes in protein-nucleic acid interactions: counterion release due to the reduction of DNA charge density and coupled folding of the protein binding site upon complexation.;We demonstrate the central importance of the polyelectrolyte character of DNA by quantifying the large differences in the binding constant ;We investigate effects of coulombic interactions and coupled folding on the binding of four extended helical and nonhelical tetravalent ;To understand the thermodynamic consequences of solute-protein interactions, we investigate interactions of bovine serum albumin (BSA) with two smaller solutes (glycine betaine and urea) in aqueous solution. Solute-BSA preferential interactions and the hydration of BSA are analyzed in terms of a general two-domain (local, bulk) model. Glycine betaine is found to be completely excluded from the first layer of hydration water surrounding BSA. Urea is found to be weakly accumulated near BSA; the extent of accumulation is proportional to urea concentration and interpretable as a weak binding interaction with polar protein surface areas.
机译:此处提出的研究解决了有关盐-核酸相互作用对配体-DNA结合的热力学效应以及溶质-蛋白质相互作用对蛋白质稳定性的影响的重要问题。模型系统用于研究蛋白质-核酸相互作用中两个主要偶联过程的热力学基础:由于DNA电荷密度的降低而释放抗衡离子,以及复合后蛋白质结合位点的偶联折叠。通过量化结合常数的巨大差异来表征DNA的聚电解质特性;我们研究库仑相互作用和偶联折叠对四个扩展的螺旋和非螺旋四价键的结合的影响;要了解溶质-蛋白质相互作用的热力学后果,我们研究牛的相互作用血清白蛋白(BSA),水溶液中含有两种较小的溶质(甘氨酸甜菜碱和尿素)。溶质-BSA优先相互作用和BSA的水合作用一般的两域(局部,本体)模型进行了分析。发现甘氨酸甜菜碱被完全排除在BSA周围的第一层水合水中。发现尿素在BSA附近微弱积聚;积累的程度与尿素浓度成正比,可以解释为与极性蛋白质表面积的弱结合相互作用。

著录项

  • 作者

    Zhang, Wentao.;

  • 作者单位

    The University of Wisconsin - Madison.;

  • 授予单位 The University of Wisconsin - Madison.;
  • 学科 Biochemistry.;Physical chemistry.
  • 学位 Ph.D.
  • 年度 1996
  • 页码 327 p.
  • 总页数 327
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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