使用恒定pH的分子动力学模拟,识别影响人体血红蛋白T/R状态构造的histidine残留物
Shin-Ichi Fujiwara1, Kotaro Nishimura1, Kazuto Imamura1
1Department of Biological Regulation, Faculty of Medicine, Tottori University, 86 Nishi-cho, Yonago 683-8503, Japan.
International journal of biological macromolecules
|April 8, 2024
概括
研究人员在人体血红蛋白中确定了特定的histidine残留物,这些残留物在生理pH下影响其T状态和R状态的构成. 这一发现促进了对血红蛋白的理解.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 蛋白质动力学 蛋白质动力学
背景情况:
- 人体血红蛋白 (Hb) 有两种主要构造:低亲和度T状态和高亲和度R状态.
- 希斯提丁 (His) 残留物的质子化状态对于调节生理pH的Hb构成至关重要.
- 确定特定的调节Hb构造的His残留物仍然是一个悬而未决的问题.
研究的目的:
- 为了研究所有38种希斯蒂丁残留物对人类血红蛋白T/R状态结构的影响.
- 在生理条件下,与特定的血红蛋白构造状态相关联的histidine质子化状态.
主要方法:
- 使用了恒定pH分子动力学 (CpHMD) 模拟.
- 在生理pH下进行模拟,以模仿生物条件.
- 专注于分析希斯蒂丁残留物的质子化状态及其对Hb结构的影响.
主要成果:
- 发现某些丁残留物的质子化状态与Hb构成相关.
- 影响形状的关键残留物包括在血附近 (α87,β92) 和子单元接口 (α89,β97) 的残留物.
- 受到histidine质子化影响的键的形成,可能解释了这种相关性.
结论:
- 特定的可定位的歇斯蒂丁残留物 (α87,α89,β92,β97) 显著影响人类血红蛋白的结构转换.
- 这些发现为控制血红蛋白氧结合特性的分子机制提供了新的见解.
- 这项研究强调了丁质子化在调节蛋白质功能的重要性.
更多相关视频
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
8.7K
11:22Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
Published on: January 30, 2018
10.1K
相关概念视频
Gene Families
8.8K
Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
8.8K
Protein and Protein Structure
79.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.5K
Globular and Fibrous Proteins
43.7K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
43.7K
