相关实验视频

Updated: Jan 11, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

30.2K

基质的结合和转移均促进了AlkB-AlkG电子转移复合体内的功能相互作用

Karolina Mikulska-Ruminska1, Matthew Licht2, Mehmed Z Ertem3

  • 1Institute of Physics, Faculty of Physics, Astronomy and Informatics, Nicolaus Copernicus University in Torun, PL 87100 Torun, Poland.

Journal of molecular biology
|November 16, 2025
PubMed
概括

阿尔干单氧化酶AlkB-AlkG复合物氧化了阿尔干. 多尺度计算揭示了多德干基质通过疏水通道的转移,影响了酶功能,并为改进的基转化提供了目标.

关键词:
阿尔干单氧化原酶是一种基.迪艾伦中心 迪艾伦中心疏水性通道的疏水性通道分子动力学模拟模拟基板转位的转位

更多相关视频

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

2.3K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.4K

相关概念视频

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.6K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.0K
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
62.9K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.4K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.4K