象域的湿形构造和水合和构造波动的密切相关性
Guorong Hu1, Haoyu Song1, Xiangjun Chen2
1School of Physics, Zhejiang University, Hangzhou 310058, China.
The journal of physical chemistry letters
|August 7, 2024
概括
内部水维持了具有类域 (PLD) 的蛋白质的动态混乱状态,防止与神经退行相关的有害聚合. 这项研究阐明了PLD如何保持灵活性,尽管有粉原性区域.
科学领域:
- 生物化学和分子生物学
- 结构生物学 结构生物学
- 神经科学是一个神经科学.
背景情况:
- 具有类域 (PLD) 的蛋白质因聚合而与神经退行性疾病有关.
- PLDs存在于类似液体的无膜有机体中,并且具有粉原性区域.
- 在凝结相中,PLDs的形状灵活性尚未得到充分理解.
研究的目的:
- 研究PLDs构造性质背后的分子机制.
- 阐明内部水在维持PLDs动态无序状态中的作用.
主要方法:
- 使用了分子动力学模拟.
- 专注于一个原型的化在肉瘤 (FUS) PLD系统.
主要成果:
- PLD采用"湿倒"形状,内部充满活跃的水分子.
- 内部水与散装环境的快速交换将蛋白质构成与水合相结合.
- 内部水的丰富性抑制了容易聚合的有序结构的形成.
结论:
- 内部水对于保持PLDs的动态,无序的形状至关重要.
- 这种水化机制抑制了PLDs的聚合倾向,为神经退行提供了洞察力.
更多相关视频
08:48High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
1.7K
09:43Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
14.2K
相关概念视频
Protein Folding
117.7K
Overview
117.7K
Conservation of Protein Domains Over Different Proteins
10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
Amyloid Fibrils
9.4K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.4K
Conservation of Protein Domains
3.1K
3.1K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
1.1K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.1K
Noncovalent Attractions in Biomolecules
49.8K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
49.8K
