神经纤维光蛋白棒域表现出结构异质性
Victoria V Nefedova1, Sergey Y Kleymenov1,2, Irina V Safenkova1
1Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
Biomolecules
|January 23, 2024
概括
神经纤维光链 (NFL) 卷-卷域表现出不同的热稳定性. 该NFL卷轴2域显示了明显的热过渡和不可逆转的变质,揭示了对全长NFL结构的洞察力.
科学领域:
- 生物化学 生物化学
- 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:
- 神经丝是关键的神经元特异性的中间丝蛋白.
- 神经纤维光链 (NFL) 是最丰富的子单元.
- 蛋白质的热稳定性是自我组装和功能的关键.
研究的目的:
- 为了研究神经纤维光链 (NFL) 卷轴-卷轴域的热稳定性.
- 分析重组NFL域及其融合的热性质.
- 了解NFL域对蛋白质整体热转换的贡献.
主要方法:
- 循环二重化谱法,以评估蛋白质结构的变化与温度.
- 差分扫描热量计用于确定热过渡温度 (Tm).
- 对重组NFL域 (NFL1B,NFL1A+1B,NFL2,NFL1B+2,NFLROD) 和它们的融合进行分析.
主要成果:
- 美国国家橄球联盟 (NFL) 的卷轴-卷轴域在各种温度范围内显示出热稳定性.
- 对于NFL1B (39.4°C),NFL1A+1B (41.9°C) 和NFL1B+2 (41.5°C) 确定了特定的Tm值.
- NFL2表现出复杂的热变质,在37.2°C和62.7°C的过渡,并经历了不可逆转的变质.
结论:
- 这项研究阐明了全长NFL的热过渡的起源.
- 结果显示,在NFL域内,特别是线圈2内,具有独特的结构性质和多样化的热稳定性.
- 了解NFL领域的热稳定性为其自我关联和整体功能提供了见解.
相关概念视频
Types of Intermediate Filaments
3.7K
The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
3.7K
The Structure of Intermediate Filaments
4.0K
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm). These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
Intermediate...
4.0K
Conservation of Protein Domains Over Different Proteins
10.9K
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...
10.9K
Assembly of Cytoskeletal Filaments
19.9K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
19.9K
Mechanism of Filopodia Formation
2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Formation of Intermediate Filaments
3.1K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.1K


