蛋白质中的酸盐-水网络的缓慢动态
R Bryn Fenwick1, David Oyen1, H Jane Dyson1
1The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
Journal of the American Chemical Society
|December 20, 2017
概括
蛋白质结合的水动力学会影响生物分子功能. 核磁共振研究揭示了蛋白质构造变化期间的水网络几何变化,影响了生物过程.
科学领域:
- 生物化学
- 结构生物学
- 生物物理
背景情况:
- 水对生物分子动力学和生物过程有重大影响.
- 微秒到毫秒 (μs-ms) 时间尺度上的蛋白质构造变化与蛋白质功能有关.
- 蛋白质结合的水在这些功能性结构变化过程中的行为仍然不太清楚.
研究的目的:
- 研究蛋白质结合的水在功能结构变化中的作用和动态.
- 通过使用NMR放松分散测量间接探测水网络动态.
- 了解水如何在结构变化过程中调解蛋白质区域之间的通信.
主要方法:
- 使用NMR放松分散测量来研究二叶酸还原酶 (DHFR) 中的三甲醇.
- 在μs-ms时间尺度结构变化过程中分析了内NH质子和环原子的化学变化.
- 综合实验化学转移与密度函数理论 (DFT) 的预测.
主要成果:
- 在结构转变过程中观察到印NH质子的显著化学转移变化,但对环的变化较小.
- 证明三英NH质子保持水结合,而周围的水网络几何变化.
- 确定放松分散可以间接地报告水动力学.
结论:
- 在μs-ms蛋白质构造变化过程中,蛋白质结合的水体几何变化是动态的.
- 水分子在功能重要蛋白质区域中传输信息方面发挥着关键作用.
- 蛋白质内部的运动可以通过蛋白质结构中的结水网络进行合.
更多相关视频
08:48High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
2.2K
12:07Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
3.8K
相关概念视频
Aquaporins
6.5K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
6.5K
Protein Diffusion in the Membrane
5.8K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
5.8K
Transcription Attenuation in Prokaryotes
18.6K
Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure. Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
18.6K
Protein Folding
128.4K
Overview
128.4K
Protein Folding
11.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.7K
Protein Dynamics in Living Cells
2.7K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.7K
