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Magnetic Fields Reduce Apoptosis by Suppressing Phase Separation of Tau-441

Research 2024年第1期2023卷 181-197页

作者： Wen-Juan Lin Wen-Pu Shi Wan-Yi Ge Liang-Liang Chen Wei-Hong Guo Peng Shang da-chuan yin Key Laboratory for Space Bioscience and Biotechnology School of Life SciencesNorthwestern Polytechnical University127 Youyixi RoadXi'an 710072ShaanxiPR China

The biological effects of magnetic fields(MFs)have been a controversial ***,in recent years,there has been increasing evidence that MFs do affect biological ***,the physical mechanism remains ***,we show that MFs(16 T)reduce apoptosis in cell lines by inhibiting liquid–liquid phase separation(LLPS)of Tau-441,suggesting that the MF effect on LLPS may be one of the mechanisms for understanding the“mysterious”magnetobiological *** LLPS of Tau-441 occurred in the cytoplasm after induction with *** phase-separated droplets of Tau-441 recruited hexokinase(HK),resulting in a decrease in the amount of free HK in the *** cells,HK and Bax compete to bind to the voltage-dependent anion channel(VdaC I)on the mitochondrial membrane.A decrease in the number of free HK molecules increased the chance of Bax binding to VdaC I,leading to increased Bax-mediated *** the presence of a static MF,LLPS was marked inhibited and HK recruitment was reduced,resulting in an increased probability of HK binding to VdaC I and a decreased probability of Bax binding to VdaC I,thus reducing Bax-mediated *** findings revealed a new physical mechanism for understanding magnetobiological effects from the perspective of *** addition,these results show the potential applications of physical environments,such as MFs in this study,in the treatment of LLPS-related diseases.

关键词： inhibited Apoptosis finding

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Recent Progresses in protein crystallogenesis in NPU

Recent Progresses in protein crystallogenesis in NPU

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第四届中国结构生物学学术讨论会

作者： da-chuan yin School of Life Sciences Northwestern Polytechnical University

Protein crystallization is an important step for structural determination of protein using X-ray crystallography. In recent decades, big advances in promoting protein crystallization have been achieved, especially with the aid of automation techniques. Due to the wide application of automation in protein crystallization, the total number of successfully resolved structures deposited in PDB database has been sharply increased to more than 88000（data on Feb 20, 2013, from http://***/pdb/home/***）. However, the overall success rate of protein crystallization from a purified soluble protein to a diffracting crystal is still at very low level, which has never exceeded 16% over the past decades. New methods to increase the success rate of protein crystallization are still necessary. In this report, I will present our recent efforts and results on protein crystallogenesis in our laboratory. The methods includes: preparation of desiccant array for gradual desiccation method to increase crystallization screening hits, dilution of crystallization agents to increase crystallization screening hits, diamagnetic levitation method to improve crystal quality, and so on.

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The Web Server Design of Ranking System for Protein Crystallization Reagents Based on the Correlation between Protein Sequence Similarity and Crystallization Reagents

The Web Server Design of Ranking System for Protein Crystall...

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第四届中国结构生物学学术讨论会

作者： Hui-Meng Lu da-chuan yin School of Life Sciences Northwestern Polytechnical University

With the increasing demands for the structural information of proteins, the data of protein 3D structures have been cumulated rapidly. However, as compared with the sequence information, the protein structural entries grew far slower. This is partly due to the bottleneck in obtaining high quality protein crystals for X-ray crystallography, which is still the main determination method for protein structure. It is essential to find out suitable crystallization conditions for proteins. However, to date there is still no rational means to aid to determine the crystallization conditions. Therefore, it is important to develop rational methods for selecting crystallization conditions so that the structural determination of proteins can be greatly enhanced. The aim may become closer when the suitable chemical reagents can be rational selected. The relationship between the protein sequence similarity and the crystallization reagents according to the information from the existing databases was analyzed. The information of reagents and sequences from the BMCD（the Biological Macromolecule Crystallization database） and the PDB database was extracted. Then the proteins were classified into different clusters according to the sequence similarity, and the relationship between the sequence similarity and the crystallization reagents was statistically analyzed. As the results, there is a pronounced positive correlation between them. Moreover, according to the correlation, a web server for predicting the feasible chemical reagents that are suitable to be used in crystallization screens and optimizations for a specific protein was designed and under internal tested. It will published soon, which named as Ranking System for Protein Crystallization Reagents. This system may help you to determine the initial condition in the optimization process, especially when you are confused in more than one condition which both gained the low-quality protein crystals after the first crystallization s

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The Possibility of Changing the Wettability of Material Surface by Adjusting Gravity

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Research 2020年第1期2020卷 435-445页

作者： Yong-Ming Liu Zi-Qing Wu Sheng Bao Wei-Hong Guo da-Wei Li Jin He Xiang-Bin Zeng Lin-Jun Huang Qin-Qin Lu Yun-Zhu Guo Rui-Qing Chen Ya-Jing Ye Chen-Yan Zhang Xu-Dong Deng da-chuan yin Key Lab of Space Bioscience&Biotechnology School of Life SciencesNorthwestern Polytechnical UniversityXi’an710072 ShaanxiChina School of Bioengineering Sichuan University of Science and EngineeringZigong643000 SichuanChina Shenzhen Research Institute of Northwestern Polytechnical University Shenzhen518057 GuangdongChina

The contact angle,as a vital measured parameter of wettability of material surface,has long been in dispute whether it is affected by ***,we measured the advancing and receding contact angles on extremely low contact angle hysteresis surfaces under different gravities(1-8G)and found that both of them decrease with the increase of the *** underlying mechanism is revealed to be the contact angle hysteresis and the deformation of the liquid-vapor interface away from the solid surface caused by gradient distribution of the hydrostatic *** real contact angle is not affected by gravity and cannot measured by an optical *** measured apparent contact angles are angles of inclination of the liquid-vapor interface away from the solid ***,a new equation is proposed based on the balance of forces acting on the three-phase contact region,which quantitatively reveals the relation of the apparent contact angle with the interfacial tensions and *** finding can provide new horizons for solving the debate on whether gravity affects the contact angle and may be useful for the accurate measurement of the contact angle and the development of a new contact angle measurement system.

关键词： apparent hysteresis hydrostatic

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Protein crystallization by mechanical vibration: improved the quality of crystals

Protein crystallization by mechanical vibration: improved th...

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第五届中国结构生物学学术讨论会

作者： Qin-Qin Lu Bin Zhang Lu Xu da-chuan yin Key Lab for Space Bioscience and Biotechnology School of Life SciencesNorthwestern Polytechnical University

Growing high quality protein crystals is always desirable for high resolution structure determination by X-ray diffraction. In this paper, we show that mechanical vibration could be an effective and useful tool to improve the quality of protein crystals. Three proteins, lysozyme, proteinase K and thaumatin, were used for the investigation, and the crystal quality of these proteins was examined using X-ray diffraction. The quality comparison of the crystals grown with and without vibration verified that mechanical vibration not only enhanced the morphology of the crystals but also improved the crystal quality. Therefore, we propose that mechanical vibration may be a useful alternative tool for obtaining good-diffracting protein crystals. Comparative analysis was conducted on all diffraction data for crystals grown with and without vibration for the three proteins. Fig. 1（a） compares of the resolution limits of all crystals of the three proteins grown with and without vibration. All the protein crystals grown with vibration demonstrated a better resolution limit than those grown in the control, and the difference in the resolution limit is not significant among the three frequency conditions. For a more reliable comparison, a one-way ANOVA test was applied to the data, and the resolution limit was normalized relative to the control data. Fig. 1（b） shows the results after the normalization and statistical tests. In terms of the resolution limits of the 164 protein crystals tested, the results indicated that, compared with the control, the crystals grown at the three frequencies all clearly possessed significantly improved resolution limits（n = 41, P = 9.75×10-7）.

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The effect of audible sound on protein crystallisation

The effect of audible sound on protein crystallisation

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中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）

作者： Chen-Yan Zhang Yan Wang Robin Schubert Christian Betzel da-chuan yin Institute for Special Environmental Biophysics Key Laboratory for Space Bioscience and BiotechnologySchool of Life SciencesNorthwestern Polytechnical University

The successful crystallisation of proteins is important because their molecular three dimensional structures can be obtained through X-ray diffraction when in their crystalline form[1].Investigation of the crystallisation process is beneficial for this *** have reported that protein crystallisation is sensitive to audible sound,which is commonly present but is often ignored.

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Sensitivity of Protein Crystallization to Concentration Change

Sensitivity of Protein Crystallization to Concentration Chan...

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中国晶体学会第五届全国会员代表大会暨学术大会（大分子分会场）

作者： Rui-Qing Chen da-chuan yin Qin-Qin Lu Jian-Yu Shi Xiao-Liang Ma School of Life Sciences Northwestern Polytechnical University

As one of the most controlled parameters in protein crystallization,the concentration of either the protein or the precipitant is closely related to the supersaturation,which is the driving force of ***,it is usually not an easy task to prepare solutions at accurate concentration levels,especially at small volumes,and it is even more difficult to prepare a series

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A general modification to the vapor diffusion protein crystallization screening

A general modification to the vapor diffusion protein crysta...

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中国晶体学会第五届全国会员代表大会暨学术大会（大分子分会场）

作者： Qin-Qin Lu Xu-Zhuo Xie Rui-Qing Chen Zi-Qing Wu da-chuan yin School of Life Sciences Northwestern Polytechnical University

It has been reported that a modification to the vapor diffusion technique,in which desiccant was used instead of reservoir solution to absorb the solvent evaporated from the crystallization droplets,increased the crystallization success ***,because the optimal amount of desiccant for a specific crystallization attempt is unknown,this desiccation method(one-time

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Recrystallization: a method to improve the quality of protein crystals

Recrystallization: a method to improve the quality of protei...

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第五届中国结构生物学学术讨论会

作者： Hai Hou Yue Liu Bo Wang Hao-Ran Tao Shan-Yang Hu da-chuan yin Key Laboratory for Space Bioscience and Biotechnology School of Life SciencesNorthwestern Polytechnical University

Recrystallization is a traditional method frequently used in materials science for the purification of metals and proteins. Because it does not alter the crystallization conditions and does not require any additional techniques. However, recrystallization is seldom considered as a feasible means to improve the quality of protein crystals. In this study, five different proteins were crystallized and recrystallized, and the crystal quality before and after recrystallization was examined by X-ray diffraction analysis. The results demonstrated that recrystallization did indeed improve crystal quality and that the crystals that grew with the recrystallization step exhibited better morphology than the initial crystals, indicating that recrystallization can be adopted as an optimization strategy for protein crystallization. Results 1. Effect of recrystallization on crystal morphology. The differences in crystal morphology demonstrated that the crystals obtained by recrystallization displayed improved morphology compared to the initially grown crystals. 2. The results of the diffraction data showed that recrystallized samples exhibited better diffraction properties than crystals obtained by the first crystallization. The crystals obtained after recrystallization exhibited higher resolution and lower mosaicity, indicating that recrystallization improved the quality of protein crystals.（a） Comparison of the resolution limits of crystals from the four different proteins obtained from the first crystallization and by recrystallization. The crystals of the best quality were chosen from each set for the comparison.（b） Statistical analysis of the resolution limits after normalization to the values found for the first crystallization（the error bars show the standard error of the mean;n = 4）. In terms of the resolution limit of the protein crystals, the results demonstrated a significant difference between the two groups（n = 4, P = 0.013, i.e. ＜0.05）. The crystals obtained by recrys

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Correlation between Protein Sequence Similarity and Crystallization Reagents in the Biological Macromolecule Crystallization database

Correlation between Protein Sequence Similarity and Crystall...

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中国晶体学会第五届全国会员代表大会暨学术大会（大分子分会场）

作者： Hui-Meng Lu da-chuan yin Yong-Ming Liu Wei-Hong Guo Ren-Bin Zhou School of Life Sciences Northwestern Polytechnical University

The protein structural entries grew far slower than the sequence *** is partly due to the bottleneck in obtaining diffraction quality protein crystals for structural determination using X-ray *** first step to achieve protein crystallization is to find out suitable chemical ***,it is not an easy *** trial and error tests of numerous

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