期刊
JOURNAL OF MOLECULAR GRAPHICS & MODELLING
卷 63, 期 -, 页码 8-14出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jmgm.2015.11.006
关键词
Hydrophobin; Protein conformation; Circular dichroism; Computer simulations; Molecular dynamics
类别
资金
- MIUR-FIRB Futuro in Ricerca [RBFR08XHOH]
- MIUR-FIRB PRIN [2010PFLRJR_005]
- Academy of Finland [276537, 260565]
- Academy of Finland (AKA) [260565, 276537, 260565, 276537] Funding Source: Academy of Finland (AKA)
Hydrophobins are proteins of interest for numerous applications thanks to their unique conformational and surface properties and their ability to self-assemble at interfaces. Here we report fully atomistic molecular mechanics and molecular dynamics results together with circular dichroism experimental data, aimed to study the conformational properties of the hydrophobin HFBII in a fluorinated solvent in comparison with a water solution and/or at an aqueous/vacuum interface. Both the atomistic simulations and the circular dichroism data show the remarkable structural stability of HFBII at all scales in all these environments, with no significant structural change, although a small cavity is formed in the fluorinated solvent. The combination of theoretical calculations and circular dichroism data can describe in detail the protein conformation and flexibility in different solvents and/or at an interface, and constitutes a first step towards the study of their self-assembly. (C) 2015 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据