相关实验视频
Updated: May 30, 2025

11:10
Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
8.3K
卡尔蛋白蛋白的蛋白质结构保护了Ni-N(他的) 债券免受竞争对手的侵害
Zhuojian Lu1, Jingyuan Nie1, Ziling Wang2
1State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.
The journal of physical chemistry letters
|January 27, 2025
概括
蛋白质环境稳定了- (Ni-N(His)) 键,这对于蛋白质净化至关重要. 与合成系统相比,这种键在蛋白质内显示出更大的机械和动力稳定性.
科学领域:
- 生物化学 生物化学
- 生物物理学的生物物理.
- 蛋白质工程是指蛋白质工程.
背景情况:
- Ni-N(His) 协调键对于使用Ni-NTA系统的重组蛋白净化至关重要.
- 以前的研究集中在合成的Ni-NTA-Histag系统上,使得蛋白质结构对键强度的影响变得不太清楚.
研究的目的:
- 为了量化生物相关蛋白质,calprotectin.His中的Ni-N(His) 键强度.
- 研究蛋白质环境对Ni-N(His) 键的机械和运动稳定性的影响.
主要方法:
- 利用基于原子力显微镜的单分子力光谱 (AFM-SMFS).
- 在calprotectin中量化破裂力和分析了Ni-N(His) 键的动态脱离率.
- 评估了对抗竞争剂和酸性条件的债券稳定性.
主要成果:
- 在calprotectin中的Ni-N(His) 键表现出大约56 pN的破裂力.
- 与合成系统相比,在蛋白质系统中观察到明显较低的脱离率,这表明稳定性得到了增强.
- 这种结合表明,易受伊米达移位的敏感性降低,在酸性条件下稳定性更强.
结论:
- 蛋白质结构在稳定Ni-N(His) 键的机械和运动性质方面发挥着至关重要的作用.
- 研究结果提供了对蛋白质内的金属-连接体相互作用的见解,以及对蛋白质净化策略的含义.
相关概念视频
Protein Folding
7.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.7K
Protein Organization
6.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.2K
Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K
Protein and Protein Structure
78.1K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
78.1K
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
Protein-protein Interfaces
12.4K
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...
12.4K

