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首页> 外文期刊>Journal of Molecular Biology >Non-native interactions in protein folding intermediates: Molecular dynamics simulations of hen lysozyme
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Non-native interactions in protein folding intermediates: Molecular dynamics simulations of hen lysozyme

机译：蛋白质折叠中间体中的非天然相互作用：鸡溶菌酶的分子动力学模拟

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Molecular dynamics simulations of protein denaturation can complement and extend experimental studies of protein folding by providing atomic-level structural information about conformational transitions and any conformational states along the unfolding pathway. Previous unfolding simulations of hen egg-white lysozyme have resulted in intermediate structures with an unfolded alpha-domain and a structured beta-domain, which is inconsistent with experiment. In contrast, the beta-domain unfolded first in the two simulations presented here leaving a structured alpha-domain. Following this, intermediate states were identified that differ with respect to the packing of the helices and the elements of non-native structure adopted. The non-native structure is critical for explaining many of the experimental observations. Overall, the pooled ensemble of these intermediates is in agreement with the experimental data for the major kinetic intermediate, suggesting that die kinetic intermediate may be made up of distinct, but rapidly interconverting, partially folded conformations distinguished primarily by differences in helix packing. (C) 1998 Academic Press. [References: 74]
机译：蛋白质变性的分子动力学模拟可通过提供有关构象转变和沿展开路径的任何构象状态的原子级结构信息，来补充和扩展蛋白质折叠的实验研究。以前的鸡蛋蛋白溶菌酶的展开模拟已导致中间结构具有未折叠的α结构域和结构化的β结构域，这与实验不一致。相反，在此处介绍的两个模拟中，β域首先展开，而剩下结构化的α域。此后，确定了中间状态，这些状态在螺旋的堆积和所采用的非本机结构的元素方面有所不同。非本地结构对于解释许多实验观察至关重要。总体而言，这些中间体的集合体与主要动力学中间体的实验数据相符，这表明该动力学中间体可能由不同的，但迅速相互转化的部分折叠的构象组成，主要由螺旋堆积的差异来区分。 （C）1998年学术出版社。 [参考：74]

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