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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Molecular motion of spin labeled side chains in the C-tenninal domain of RGL2 protein: A SDSL-EPR and MD study
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Molecular motion of spin labeled side chains in the C-tenninal domain of RGL2 protein: A SDSL-EPR and MD study

机译：RGL2蛋白C末端结构域中自旋标记侧链的分子运动：SDSL-EPR和MD研究

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摘要

Five singly spin labeled side chains at surface sites in the C-terminal domain of RGL2 protein have been analyzed to investigate the general relationship between nitroxide side chain mobility and protein structure. At these sites, the structural perturbation produced by replacement of a native residue with a nitroxide side chain appears to be very slight at the level of the backbone fold. The primary determinants of the nitroxide side chain mobility are backbone dynamics and tertiary interactions. On the exposed surfaces of a-helices, the side chain mobility is not restricted by tertiary interactions but appears to be determined by backbone dynamics, while in loop sites, the side chain mobility is even higher. For a better understanding of the changes in the EPR spectral line shape, molecular dynamics simulations were performed and found in agreement with EPR spectral data. (c) 2006 Elsevier B.V. All rights reserved.
机译：分析了RGL2蛋白C末端结构域表面位点的五个单旋标记侧链，以研究氮氧化物侧链迁移率与蛋白质结构之间的一般关系。在这些位点上，通过用氮氧化物侧链替换天然残基而产生的结构扰动在主链折叠水平上似乎非常轻微。氮氧化物侧链迁移率的主要决定因素是主链动力学和三级相互作用。在α-螺旋的暴露表面上，侧链迁移率不受三次相互作用的限制，而似乎由骨架动力学决定，而在环状位点，侧链迁移率甚至更高。为了更好地了解EPR谱线形状的变化，进行了分子动力学模拟，发现与EPR谱数据一致。 （c）2006 Elsevier B.V.保留所有权利。

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