相关实验视频
Updated: Jul 11, 2025

11:14
Primer-Free Aptamer Selection Using A Random DNA Library
Published on: July 26, 2010
24.9K
从低强度选择中分离出来的XNA Aptamers的约束性质的参数化.
Nandini Kundu1, Cailen M McCloskey1, Mohammad Hajjar1
1Department of Pharmaceutical Sciences, University of California, Irvine, California 92697-3958, United States.
Biochemistry
|November 6, 2023
概括
这项研究量化了阿帕特马结合亲和力,揭示了针对特定标的三核酸 (TNA) 阿帕特马的狭窄范围 (1-15 nM KD). 这些发现有助于确定胺体发现的较低结合极限.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 生物信息学是一种生物信息学.
背景情况:
- 机器学习有助于体发现,但需要关于结合亲和度范围的实验数据.
- 了解较低的结合亲和度极限对于区分阿普坦与非结合剂至关重要.
研究的目的:
- 量化探索体的多样性,并确定较低的结合亲和度极限.
- 为aptamer发现算法提供实验约束.
主要方法:
- 在实验室中选择三核酸 (TNA) 受体对抗受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体受体
- 选择的aptamer库的高密度测序. 选择的aptamer库的高密度测序.
- 对136个分离的TNA体进行动力分析,以确定平衡分离常数 (KD).
主要成果:
- 在两个实验复制物之间观察到一个一致的,狭窄的平衡解离常数范围 (KD ≈ 1-15 nM).
- 该研究描述了在低强度条件下产生的TNA体的结合亲和力.
结论:
- 这些发现提供了对阿普坦对抗无原性标的较低结合亲和度极限的见解.
- 这些数据可以为开发更有效的aptamer发现算法和实验评估提供信息.
相关概念视频
The Equilibrium Binding Constant and Binding Strength
13.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
13.0K
Ligand Binding Sites
12.9K
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...
12.9K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K

