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相关概念视频

Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Overview
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Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

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Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
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The Equilibrium Binding Constant and Binding Strength02:18

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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:
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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.
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Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
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Application of Elemental Lanthanides in the Selective C-F Activation of Trifluoromethylated Benzofulvenes Providing Access to Various Difluoroalkenes
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兰莫杜林:一种使用兰酸的细菌的高度选择性的兰酸结合蛋白

Joseph A Cotruvo1, Emily R Featherston1, Joseph A Mattocks1

  • 1Department of Chemistry , The Pennsylvania State University , University Park , Pennsylvania 16802 , United States.

Journal of the American Chemical Society
|October 24, 2018
PubMed
概括

研究人员发现了兰莫杜林 (LanM),一种选择性地通过离子结合兰化物 (Lns) 的蛋白质. 这一发现揭示了有机体如何区分这些金属,并提供了潜在的生物技术应用.

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科学领域:

  • 生物化学
  • 微生物学
  • 生物技术

背景情况:

  • 兰化物 (Lns) 越来越多地被认为是甲基培养细菌酶中的必需辅助因子.
  • 了解选择性金属离子结合的生物机制对于基础科学和技术应用都至关重要.

研究的目的:

  • 识别和表征一种负责选择性胺结合的Methylobacterium extorquens中的蛋白质.
  • 阐明兰化物对的选择性的结构和功能基础.

主要方法:

  • 兰莫杜林 (LanM) 的蛋白质净化和表征.
  • 金属结合测试以确定和的亲和性和选择性.
  • 对LanM的局部定向突变,以调查特定残留物在金属选择性中的作用.

主要成果:

  • 兰莫杜林 (LanM) 的鉴定,一种具有四个EF手动图案的新型蛋白质,可在皮科莫尔度下选择性地结合兰化物 (LnIII).
  • 在LnIII结合时,LanM会发生显著的形状变化,从无序状态转变为有序状态.
  • 在LanM的EF手中独特的プロ林残留物的突变改变了 (CaII) 与微分子范围的结合,同时保持了高的LnIII亲缘关系,突出了它们在选择性中的作用.

结论:

  • 兰莫杜林 (LanM) 是一种高度选择性的化物结合蛋白,对于理解生物金属离子识别至关重要.
  • 在LanM的EF手中,独特的类残留物是类对类选择性的关键决定因素.
  • 这一发现对开发用于化物检测,封存和分离的生物技术有影响.