相关实验视频

Updated: Jul 16, 2026

Collecting Variable-concentration Isothermal Titration Calorimetry Datasets in Order to Determine Binding Mechanisms
10:04

Collecting Variable-concentration Isothermal Titration Calorimetry Datasets in Order to Determine Binding Mechanisms

Published on: April 7, 2011

评价Nitrosylcobalamin与内在因子的结合亲和力,作为Cobalamin结合蛋白相互作用的预测模型:与Hydroxocobalamin进行比较研究

Annette M Sysel1, Joseph A Bauer2

  • 1Bauer Research Foundation, Inc., Akron, OH 44312, USA.

Frontiers in bioscience (Elite edition)
|March 28, 2025
PubMed
概括

尼甲胺 (NO-Cbl) 和甲胺 (OH-Cbl) 强烈与内在因子 (IF) 结合,OH-Cbl的亲和力略高. 植物衍生IF是评估可巴拉胺模拟结合和治疗潜力的合适模型.

关键词:
科巴拉胺是什么意思氧巴胺 (OH-Cbl) 是一种维生素B12的成分.内在因素 (IF) 是一个内在因素.氧化 (NO) 是一种氧化.尼特基巴胺 (NO-Cbl) 是一种基巴胺.表面等离子体共振 (SPR) 是一种表面等离子体共振.

更多相关视频

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

The Caco-2 Cell Bioassay for Measurement of Food Iron Bioavailability06:34

The Caco-2 Cell Bioassay for Measurement of Food Iron Bioavailability

Published on: April 28, 2022

相关概念视频

Ligand Binding Sites02:40

Ligand Binding Sites

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...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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:
Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...