関連する実験動画

Updated: Jul 25, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

タンパク質阻害剤複合体の結合自由エネルギーの相対変化の計算

P A Bash, U C Singh, F K Brown

    Science (New York, N.Y.)
    |January 30, 1987
    PubMed
    まとめ

    分子ダイナミクスシミュレーションは,熱解シン阻害剤の自由エネルギー結合を正確に予測しました. この計算方法は,酵素-阻害剤の相互作用を理解するのに役立ちますし,タンパク質と薬物の設計を導くことができます.

    さらに関連する動画

    Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions10:44

    Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

    Published on: October 21, 2016

    Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors10:29

    Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

    Published on: May 9, 2025

    関連する概念動画

    Calculating Standard Free Energy Changes02:49

    Calculating Standard Free Energy Changes

    The free energy change for a reaction that occurs under the standard conditions of 1 bar pressure and at 298 K is called the standard free energy change. Since free energy is a state function, its value depends only on the conditions of the initial and final states of the system. A convenient and common approach to the calculation of free energy changes for physical and chemical reactions is by use of widely available compilations of standard state thermodynamic data. One method involves the...
    Free Energy and Equilibrium02:56

    Free Energy and Equilibrium

    The free energy change for a process may be viewed as a measure of its driving force. A negative value for ΔG represents a driving force for the process in the forward direction, while a positive value represents a driving force for the process in the reverse direction. When ΔGrxn is zero, the forward and reverse driving forces are equal, and the process occurs in both directions at the same rate (the system is at equilibrium).
    Recall that Q is the numerical value of the mass action expression...
    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...