当前位置: X-MOL 学术Prog. Biophys. Mol. Biol. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Stability of multi-subunit proteins and conformational lock.
Progress in Biophysics and Molecular Biology ( IF 3.8 ) Pub Date : 2019-08-27 , DOI: 10.1016/j.pbiomolbio.2019.08.008
L Alaei 1 , Ali A Moosavi-Movahedi 2
Affiliation  

One of the important physicochemical features of the proteins specifically multi-subunit types is their stability at high temperatures. The kinetics of the dissociation and denaturation of proteins possessing at least two subunits has certain challenges because the overall mechanism of dissociation can include hidden reversible and/or irreversible steps (conformational lock). There are numerous proteins related to diseases which are in equilibrium with oligomer forms. This equilibrium plays an important role in holding the activity levels of these proteins in vitro and in vivo. The stability of proteins is an essential milestone to study conformational changes of the proteins in the living cell. This concept is of great importance when proteins are used in biomedicine fields. The quaternary structure of multi-subunit proteins includes properties that affect function and kinetics of denaturation. The kinetics of denaturation may include some hidden stages of conformational transitions in the protein and steps of reversible dissociation of the oligomer. The transforming factors affect different areas especially active centers in the clefts of each subunit. The distinctive agent among all, is the temperature which sequentially destructs independent inter-subunit contact sites. Recent experimental data regarding dissociative mechanism for irreversible thermal denaturation of multi-subunit proteins have been summarized in the present paper.



中文翻译:

多亚基蛋白的稳定性和构象锁定。

蛋白质特别是多亚基类型的重要物理化学特征之一是其在高温下的稳定性。具有至少两个亚基的蛋白质的解离和变性动力学具有某些挑战,因为解离的总体机制可能包括隐藏的可逆和/或不可逆步骤(构象锁)。有许多与疾病有关的蛋白质与寡聚体形式处于平衡状态。这种平衡在保持体内和体外这些蛋白质的活性水平方面起着重要作用。蛋白质的稳定性是研究活细胞中蛋白质构象变化的重要里程碑。当蛋白质用于生物医学领域时,这一概念非常重要。多亚基蛋白的四级结构包括影响变性功能和动力学的特性。变性的动力学可以包括蛋白质中构象转变的一些隐藏阶段和寡聚物的可逆解离步骤。转化因子影响不同区域,尤其是每个亚基裂隙中​​的活性中心。其中最有特色的是顺序破坏独立的亚基间接触部位的温度。本文总结了有关多亚基蛋白不可逆热变性的解离机理的最新实验数据。变性的动力学可以包括蛋白质中构象转变的一些隐藏阶段和寡聚物的可逆解离步骤。转化因子影响不同区域,尤其是每个亚基裂隙中​​的活动中心。其中最有特色的是顺序破坏独立的亚基间接触部位的温度。本文总结了有关多亚基蛋白不可逆热变性的解离机理的最新实验数据。变性的动力学可以包括蛋白质中构象转变的一些隐藏阶段和寡聚物的可逆解离步骤。转化因子影响不同区域,尤其是每个亚基裂隙中​​的活动中心。其中最有特色的是顺序破坏独立的亚基间接触部位的温度。本文总结了有关多亚基蛋白不可逆热变性的解离机理的最新实验数据。

更新日期:2019-08-27
down
wechat
bug