当前位置: X-MOL 学术bioRxiv. Biochem. › 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.)
Conformational Dynamics of NSP11 Peptide of SARS-CoV-2 Under Membrane Mimetics and Different Solvent Conditions
bioRxiv - Biochemistry Pub Date : 2021-01-19 , DOI: 10.1101/2020.10.07.330068
Kundlik Gadhave , Prateek Kumar , Ankur Kumar , Taniya Bhardwaj , Neha Garg , Rajanish Giri

The intrinsically disordered proteins/regions (IDPs/IDPRs) are known to be responsible for multiple cellular processes and are associated with many chronic diseases. In viruses, the existence of a disordered proteome is also proven and is related to its conformational dynamics inside the host. The SARS-CoV-2 has a large proteome, in which, structure and functions of many proteins are not known yet, along with nsp11. In this study, we have performed extensive experimentation on nsp11. Our results based on the CD spectroscopy gives characteristic disordered spectrum for IDPs. Further, we investigated the conformational behavior of nsp11 in the presence of membrane mimetic environment, α-helix inducer, and natural osmolyte. In the presence of negatively charged and neutral liposomes, nsp11 remains disordered. However, with SDS micelle, it adopted an α-helical conformation, suggesting the helical propensity of nsp11. Finally, we again confirmed the IDP behavior of nsp11 using MD simulations. In future, this conformational dynamic study could help to clarify its functional importance in SARS-CoV-2 infection.

中文翻译:

膜模拟和不同溶剂条件下SARS-CoV-2 NSP11肽的构象动力学

已知内在无序的蛋白质/区域(IDP / IDPR)负责多种细胞过程,并与许多慢性疾病有关。在病毒中,蛋白质组紊乱的存在也得到了证明,并与其在宿主内部的构象动力学有关。SARS-CoV-2具有较大的蛋白质组,其中许多蛋白质的结构和功能以及nsp11尚不清楚。在这项研究中,我们对nsp11进行了广泛的实验。我们基于CD光谱的结果给出了IDP的特征无序光谱。此外,我们研究了在膜模拟环境,α-螺旋诱导剂和天然渗透压剂存在下nsp11的构象行为。在带负电荷和中性脂质体的情况下,nsp11仍然处于混乱状态。但是,对于SDS胶束,它采用α-螺旋构象,表明nsp11的螺旋倾向。最后,我们再次使用MD模拟确认了nsp11的IDP行为。将来,这种构象动力学研究可能有助于阐明其在SARS-CoV-2感染中的功能重要性。
更新日期:2021-01-20
down
wechat
bug