JoVE - Journal of Visualized Experiments
JoVE Visualize
Contact Us
这页已由机器翻译。其他页面可能仍然显示为英文。 View in English

揭示了结吸附的物理化学

  • 0Instituto de Investigaciones Fisicoquímicas, Teóricas y Aplicadas (INIFTA), UNLP-CONICET, La Plata, Argentina.
Journal of Colloid and Interface Science +

|

2025年九月6日

在PubMed上查看摘要

概括

此摘要是机器生成的。

相关概念视频

Silica Gel Column Chromatography: Overview 01:10

1.7K

Silica gel column chromatography is a technique for separating compounds using a column packed with silica gel as the stationary phase. This method relies on differences in the polarity of compounds. Based on their polarities, compounds move between the stationary phase (silica gel) and the mobile phase (the solvent), forming discrete bands in the column.
Polar components tend to bind strongly to the silica gel, causing them to move slowly through the column. In contrast, nonpolar compounds...

Noncovalent Attractions in Biomolecules 02:35

54.4K

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,...

The Equilibrium Binding Constant and Binding Strength 02:18

13.4K

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:

where  P and L are the unbound protein and ligand, respectively, and PL is the protein-ligand complex. 
As the amount of bound ligand is also related to the rate of ligand binding, experiments can also determine Kb by examining the rates of protein-ligand association (kon) and dissociation (koff) using the following ratio:

Ligand Binding Sites 02:40

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...