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相关概念视频

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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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:
12.8K
The Nernst Equation02:59

The Nernst Equation

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Nonstandard Reaction Conditions
The interconnection between standard cell potentials and various thermodynamic parameters such as the standard free energy change ΔG° and equilibrium constant K has been previously explored. For example, a redox reaction involving zinc(II) and tin(II) ions at 1 M concentration with Eºcell = +0.291 V and ΔG° = −56.2 kJ is spontaneous.
40.2K
Redox Equilibria: Overview01:23

Redox Equilibria: Overview

522
A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
522
Conserved Binding Sites01:49

Conserved Binding Sites

4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Calculating Standard Free Energy Changes02:49

Calculating Standard Free Energy Changes

20.7K
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...
20.7K
Gibbs Free Energy and Thermodynamic Favorability02:23

Gibbs Free Energy and Thermodynamic Favorability

6.7K
The spontaneity of a process depends upon the temperature of the system. Phase transitions, for example, will proceed spontaneously in one direction or the other depending upon the temperature of the substance in question. Likewise, some chemical reactions can also exhibit temperature-dependent spontaneities. To illustrate this concept, the equation relating free energy change to the enthalpy and entropy changes for the process is considered:
6.7K

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相关实验视频

Updated: Jun 4, 2025

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
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基于RED-E函数的平衡参数寻找器:在绝对约束的自由能量计算中找到最佳的限制参数.

Wanyi Huang1, Runduo Liu1, Yufen Yao1

  • 1State Key Laboratory of Anti-Infective Drug Discovery and Development, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.

The journal of physical chemistry letters
|December 24, 2024
PubMed
概括

本研究引入了一种新方法,即REPF,用于优化具有约束力的自由能源计算中的限制. REPF显著降低了计算成本,同时保持了对联体蛋白结合亲缘关系的预测准确度.

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

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科学领域:

  • 计算化学是一种计算化学.
  • 分子建模分子建模
  • 药物发现 药物发现

背景情况:

  • 基于自由能量扰动 (FEP) 的绝对结合自由能量 (ABFE) 计算对于预测联体蛋白结合亲和关系至关重要.
  • 在FEP-ABFE中优化紧固件的添加是具有挑战性的,因为非直角合器,需要许多模拟 (λ窗口).

研究的目的:

  • 引入一种新的方法,即基于RED-E功能的平衡参数查找器 (REPF),用于优化限制平衡值.
  • 为了在FEP-ABFE计算中改善相位重叠和收时的限制添加.

主要方法:

  • REPF使用波束来优化平衡值.
  • 该方法应用于5个目标中的44个蛋白质-连接体复合体.
  • 优化REPF的限制与现有的文献限制计划进行了比较.

主要成果:

  • 仅使用2λ模拟,REPF实现了与12λ方法相比的准确性.
  • 这代表了计算成本的显著降低.
  • 广泛的测试证实了REPF优化约束装置的改进趋同和减少能量波动.

结论:

  • 在FEP-ABFE计算中,REPF提供了一种更有效的限制优化方法.
  • 该方法提高了准确性,并减少了药物发现中的计算需求.
  • REPF是一个有价值的工具,可以加速预测绑定亲和关系.