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来自……的核糖体蛋白L25中三种不同α螺旋的分子动力学 。 你提供的原文似乎不完整，“from”后面缺少具体信息。

Molecular dynamics of three different α-helices in ribosomal protein L25 from .

作者信息

Chirgadze Yuri, Likhachev Ilya, Balabaev Nikolai, Brazhnikov Evgeniy

机构信息

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.

Institute of Mathematical Problems of Biology, Branch of Keldysh Institute of Applied Mathematics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.

出版信息

Biochem Biophys Rep. 2024 Sep 29;40:101836. doi: 10.1016/j.bbrep.2024.101836. eCollection 2024 Dec.

DOI:10.1016/j.bbrep.2024.101836
PMID:39403096
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11472105/
Abstract

A true native protein state is realized in a water solution where proteins exhibit their dynamic properties important for the functioning. This is way we have analyzed the dynamics of α-helices inside ribosomal protein L25 from in a water solution. The dynamics of only main chain Cα-atoms have been simulated along the five independent trajectories at a total time 200ns. Superposed average dynamics picture of L25 structure coincides very well with the NMR protein structure in a water solution. Dynamic shifts of Cα-atoms of the α-helices are related with a restraint status of the residue side chain. In contrast, Cα-atoms of the β-sheet, which form a hydrophobic core, show very low dynamic motion and higher stability. Dynamic specificity of the main chain of protein L25 could explain its particular features in the complex with 5S rRNA and in the structure of the ribosome.

摘要

真正的天然蛋白质状态是在水溶液中实现的，蛋白质在其中展现出对其功能至关重要的动态特性。这就是我们分析核糖体蛋白L25内部α-螺旋在水溶液中的动力学的原因。仅沿着五条独立轨迹在总时长200纳秒内模拟了主链Cα原子的动力学。L25结构的叠加平均动力学图像与水溶液中的核磁共振蛋白质结构非常吻合。α-螺旋的Cα原子动态位移与残基侧链的受限状态有关。相比之下，形成疏水核心的β-折叠的Cα原子显示出非常低的动态运动和更高的稳定性。蛋白质L25主链的动态特异性可以解释其在与5S rRNA形成的复合物以及核糖体结构中的特殊特征。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/eea4b69ff352/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/5c85b49bcf16/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/58bba5715d9d/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/fc91fe2c518c/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/5dba9bf55ef2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/eea4b69ff352/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/5c85b49bcf16/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/58bba5715d9d/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/fc91fe2c518c/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/5dba9bf55ef2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bb96/11472105/eea4b69ff352/gr5.jpg

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