関連する実験動画

Updated: Mar 19, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.4K

分子ノードによるアロステリック誘導と触媒の調節

Vanesa Marcos1, Alexander J Stephens1, Javier Jaramillo-Garcia1

  • 1School of Chemistry, University of Manchester, Oxford Road, Manchester, M13 9PL, UK.

Science (New York, N.Y.)
|June 25, 2016
PubMed
まとめ

化学反応を制御する 合成分子ペンタフォイルノートを 開発しました この分子結合戦略は鎖の形状を制限し,結合していない分子では見られないユニークな触媒機能を可能にします.

さらに関連する動画

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K
Modeling an Enzyme Active Site using Molecular Visualization Freeware14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

11.8K

関連する概念動画

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
11.3K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.2K
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...
64.3K
Allosteric Regulation01:08

Allosteric Regulation

16.1K
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...
9.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.8K