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Effect of water and polyols on the dynamics of lysozyme studied by solid-state NMR.

机译：固态NMR研究了水和多元醇对溶菌酶动力学的影响。

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摘要

One of the main goals of protein research is to understand the relationship between protein structure, dynamics, and function. The purpose of this dissertation is to investigate dynamic heterogeneity and the effects of water and polyols on dynamics and the dynamical transition in lysozyme using nuclear magnetic resonance (NMR) spectroscopy and electrospray ionization mass spectrometry (ESI-MS).{09}; Both 13CH3-labeled and C 2H3-labeled lysozyme were investigated to explore dynamics at the protein surface. 13C CP-MAS solid state NMR spectra showed an improvement in spectral resolution on addition of water reflecting both a decrease in the distribution of isotropic chemical shifts, as preferred conformations are populated on hydration, as well as contributions from motional averaging of chemical shift anisotropy and dipolar coupling interactions. With increasing temperature and hydration, a change in 2H NMR spectral line shape was observed for lysine residues labeled with C 2H3 groups indicating the onset of a new motion at the melting point of water suggesting that the dynamic properties of protein surface groups are strongly coupled to those of the solvent.; In order to explore the dynamic heterogeneity of the protein interior, a solid-state 2H NMR study of a series of dry and hydrated lysozyme samples kinetically labeled by hydrogen isotope exchange so as to select regions of the protein interior with different isotope exchange rates has been conducted. Samples deuterated on the slowest exchanging sites or on the protein surface gave essentially the same line shape indicating that all peptide sites within the protein undergo the same type of motion with similar amplitudes. Interestingly, spin lattice relaxation times (T1 ) for the dry protein are found to correlate with the exchange rates of sites in the hydrated protein. Hydration leads to a significant decrease in T1 even for sites in the slow-exchange core. A mechanism involving small amplitude rigid-body fluctuations of the slow-exchange core within the plasticized protein matrix is proposed to explain this behavior.
机译：蛋白质研究的主要目标之一是了解蛋白质结构，动力学和功能之间的关系。本文的目的是利用核磁共振（NMR）光谱和电喷雾电离质谱（ESI-MS）研究动态异质性以及水和多元醇对溶菌酶动力学和动力学转变的影响。{09}；研究了13CH3标记和C 2H3标记的溶菌酶，以探索蛋白质表面的动力学。 13C CP-MAS固态NMR光谱显示，添加水后光谱分辨率有所提高，这反映了各向同性化学位移的分布减少，这是因为在水化过程中出现了优选的构象，以及化学位移各向异性和偶极耦合相互作用。随着温度和水合作用的增加，观察到标记为C 2H3基团的赖氨酸残基的2H NMR谱线形状发生变化，表明在水的熔点处开始出现新的运动，这表明蛋白质表面基团的动态特性与那些溶剂。为了探索蛋白质内部的动态异质性，已进行了一系列氢同位素交换动力学标记的干燥和水合溶菌酶样品的固态2H NMR研究，从而选择了具有不同同位素交换速率的蛋白质内部区域进行。在最慢的交换位点或蛋白质表面上氘化的样品基本上具有相同的线形，这表明蛋白质内的所有肽位点均以相同的幅度经历相同类型的运动。有趣的是，干燥蛋白质的自旋晶格弛豫时间（T1）与水合蛋白质中位点的交换速率相关。水合导致T1显着降低，即使对于慢交换核心中的位点也是如此。提出了一种机制，该机制涉及增塑蛋白基质中慢交换核心的小幅度刚体波动，以解释这种行为。

著录项

  • 作者

    Li, Gang.;

  • 作者单位

    Kent State University.;

  • 授予单位 Kent State University.;
  • 学科 Chemistry Analytical.; Chemistry Polymer.; Biophysics General.
  • 学位 Ph.D.
  • 年度 2006
  • 页码 150 p.
  • 总页数 150
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;高分子化学（高聚物）;生物物理学;
  • 关键词

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