疏水不匹配调整α-螺旋和细胞膜之间的相互作用动力学
Zijian Ni1, Jing Lai1, Shuji Ye1
1Hefei National Research Center for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230026, China.
Langmuir : the ACS journal of surfaces and colloids
|August 27, 2025
概括
和脂质双层之间的疏水不匹配增加了自由能量,降低了插入和相互作用率. 本研究量化了这种不匹配对膜相互作用的影响.
科学领域:
- 生物物理
- 膜生物物理
- 蛋白质与脂质的相互作用
背景情况:
- 蛋白质和脂质双层之间的疏水不匹配在能量上是不利的.
- 疏水不匹配对相互作用自由能量和动力学的影响尚不清楚.
研究的目的:
- 调查疏水不匹配如何影响和脂质双层之间的相互作用的自由能量.
- 量化疏水不匹配对膜相互作用动力学的影响.
主要方法:
- 使用KALP23模型的总频率生成振动光谱 (SFG-VS).
- 检查了不同疏水厚度的脂双层相互作用.
主要成果:
- 疏水性不匹配显著影响的插入深度和方向.
- 增加的不匹配导致多余的自由能量,使数和跨膜相互作用率呈指数下降.
- SFG系统没有改变的倾斜角度或相对分子数.
结论:
- 疏水性不匹配是调整膜相互作用动态的一个关键因素.
- 这些发现提高了对细胞膜内的理解.
相关概念视频
Protein-protein Interfaces
13.2K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
13.2K
Ligand Binding Sites
13.1K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
13.1K
Asymmetric Lipid Bilayer
7.7K
Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
7.7K
Multi-pass Transmembrane Proteins and β-barrels
5.5K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.5K
Protein Folding
120.8K
Overview
120.8K
Membrane Fluidity
155.7K
Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
155.7K


