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2.
Research (Wash D C) ; 2020: 2640834, 2020.
Article in English | MEDLINE | ID: mdl-32043083

ABSTRACT

The contact angle, as a vital measured parameter of wettability of material surface, has long been in dispute whether it is affected by gravity. Herein, 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 gravity. 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 pressure. The real contact angle is not affected by gravity and cannot measured by an optical method. The measured apparent contact angles are angles of inclination of the liquid-vapor interface away from the solid surface. Furthermore, 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 gravity. This 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.

3.
Article in Chinese | WPRIM (Western Pacific) | ID: wpr-702184

ABSTRACT

Objective To investigate whether paraquat (PQ) induced rat alveolar type Ⅱ cells (RLE-6TN) epithelial-mesenchymal transition(EMT) and explore the underlying molecular mechanism.Methods RLE-6TN cells were treated by 20 μmol/L PQ for 24 hours,the morphology was observed by invert microscope.RT-PCR and Western blot were performed to detect the expression level of β-catenin,EMT related markers E-cadherin and vimentin.Then we performed the Transwell invasion assays to detect the ability of cell invasion.Results The results demonstrated that PQ was able to induce the transition of RLE-6TN cells from epithelial morphology to fibroblast-like morphology,associated with the acquisition of migratory properties.Furthermore,knockdown of β-catenin by using specific siRNA could reverse PQ triggered EMT process and attenuated cell migration ability.Conclusion PQ promotes RLE-6TN epithelial-mesenchymal transition by upregulating the expression of Wnt/β-catenin.

4.
Sci Rep ; 4: 7308, 2014 Dec 04.
Article in English | MEDLINE | ID: mdl-25471817

ABSTRACT

High-quality protein crystals of suitable size are an important prerequisite for applying X-ray crystallography to determine the 3-dimensional structure of proteins. However, it is often difficult to obtain protein crystals of appropriate size and quality because nucleation and growth processes can be unsuccessful. Here, we show that by adsorbing proteins onto porous polystyrene-divinylbenzene microspheres (SDB) floating on the surface of the crystallisation solution, a localised high supersaturation region at the surface of the microspheres and a low supersaturation region below the microspheres can coexist in a single solution. The crystals will easily nucleate in the region of high supersaturation, but when they grow to a certain size, they will sediment to the region of low supersaturation and continue to grow. In this way, the probability of crystallisation and crystal quality can be simultaneously increased in a single solution without changing other crystallisation parameters.

5.
Acta Crystallogr D Biol Crystallogr ; 69(Pt 10): 1901-10, 2013 Oct.
Article in English | MEDLINE | ID: mdl-24100310

ABSTRACT

High-quality crystals are key to obtaining accurate three-dimensional structures of proteins using X-ray diffraction techniques. However, obtaining such protein crystals is often a challenge. Several containerless crystallization techniques have been reported to have the ability to improve crystal quality, but it is unknown which is the most favourable way to grow high-quality protein crystals. In this paper, a quality comparison of protein crystals which were grown under three containerless conditions provided by diamagnetic levitation, silicone oil and agarose gel was conducted. A control experiment on a vessel wall was also simultaneously carried out. Seven different proteins were crystallized under the four conditions, and the crystal quality was assessed in terms of the resolution limit, the mosaicity and the Rmerge. It was found that the crystals grown under the three containerless conditions demonstrated better morphology than those of the control. X-ray diffraction data indicated that the quality of the crystals grown under the three containerless conditions was better than that of the control. Of the three containerless crystallization techniques, the diamagnetic levitation technique exhibited the best performance in enhancing crystal quality. This paper is to our knowledge the first report of improvement of crystal quality using a diamagnetic levitation technique. Crystals obtained from agarose gel demonstrated the second best improvement in crystal quality. The study indicated that the diamagnetic levitation technique is indeed a favourable method for growing high-quality protein crystals, and its utilization is thus potentially useful in practical efforts to obtain well diffracting protein crystals.


Subject(s)
Crystallography, X-Ray , Gravitation , Magnetic Resonance Spectroscopy , Photoelectron Spectroscopy , Proteins/chemistry , Sepharose/standards , Silicone Oils/standards , Animals , Chickens , Crystallization/methods , Crystallization/standards , Crystallography, X-Ray/methods , Crystallography, X-Ray/standards , Escherichia coli Proteins/chemistry , Proteins/standards , Quality Control , Trichosanthes , X-Ray Diffraction/methods , X-Ray Diffraction/standards
6.
Article in English | MEDLINE | ID: mdl-23832217

ABSTRACT

The pH of a solution is an important parameter in crystallization that needs to be controlled in order to ensure success. The actual pH of the crystallization droplet is determined by the combined contribution of the buffers in the screening and protein solutions, although the contribution of the latter to the pH is often ignored. In this study, the effects of the buffer and protein solution pH values on the results of screening are systematically investigated. It was found that these parameters significantly affected the results and thus the following strategy for the selection of appropriate pH values is proposed: (i) when screening with only one protein solution, the pH should be as low, as high or as divergent from the pI as possible for a basic, acidic or neutral protein, respectively, within its stable pH range; (ii) when screening with two protein solutions, the pH values should be well separated from one another; and (iii) when multiple pH values are utilized, an even distribution of pH values is the best approach to increase the success rate of crystallization.


Subject(s)
Proteins/chemistry , Solutions/chemistry , Buffers , Crystallization , Hydrogen-Ion Concentration
7.
Int J Mol Sci ; 14(6): 12329-45, 2013 Jun 07.
Article in English | MEDLINE | ID: mdl-23749116

ABSTRACT

Most protein crystallisation begins from heterogeneous nucleation; in practice, crystallisation typically occurs in the presence of a solid surface in the solution. The solid surface provides a nucleation site such that the energy barrier for nucleation is lower on the surface than in the bulk solution. Different types of solid surfaces exhibit different surface energies, and the nucleation barriers depend on the characteristics of the solid surfaces. Therefore, treatment of the solid surface may alter the surface properties to increase the chance to obtain protein crystals. In this paper, we propose a method to modify the glass cover slip using a self-assembled monolayer (SAM) of functional groups (methyl, sulfydryl and amino), and we investigated the effect of each SAM on protein crystallisation. The results indicated that both crystallisation success rate in a reproducibility study, and crystallisation hits in a crystallisation screening study, were increased using the SAMs, among which, the methyl-modified SAM demonstrated the most significant improvement. These results illustrated that directly modifying the crystallisation plates or glass cover slips to create surfaces that favour heterogeneous nucleation can be potentially useful in practical protein crystallisation, and the utilisation of a SAM containing a functional group can be considered a promising technique for the treatment of the surfaces that will directly contact the crystallisation solution.


Subject(s)
Proteins/chemistry , Adsorption , Chemical Precipitation , Crystallization , Microscopy, Atomic Force , Models, Molecular , Photoelectron Spectroscopy , Reproducibility of Results , Silanes/chemistry , Spectroscopy, Fourier Transform Infrared
8.
J Acoust Soc Am ; 131(4): 3164-72, 2012 Apr.
Article in English | MEDLINE | ID: mdl-22501088

ABSTRACT

This paper reports on an ultrasonic levitation system developed for crystallization from solution in a containerless condition. The system has been proven to be able to levitate droplets stably and grow crystals rapidly and freely from a levitated droplet. Crystals of four samples, including NaCl, NH(4)Cl, lysozyme, and proteinase K, were obtained successfully utilizing the system. The studies showed that the crystals obtained from the acoustically levitated droplets all exhibited higher growth rates, larger sizes, better shapes, fewer crystals, as well as fewer twins and shards, compared with the control on a vessel wall. The results indicated that containerless ultrasonic levitation could play a key role in improving the crystallization of both inorganic salts and proteins. The ultrasonic levitation system could be used as a ground-based microgravity simulation platform, which could swiftly perform crystallization and screening of crystallization conditions for space crystallization and other ground-based containerless techniques. Moreover, the approach could also be conveniently applied to researching the dynamics and mechanism of crystallization. In addition, the device could be used for the preparation of high-purity materials, analysis of minute or poisonous samples, study of living cells, environmental monitoring, and so on.

9.
Int J Mol Sci ; 13(12): 16916-28, 2012 Dec 11.
Article in English | MEDLINE | ID: mdl-23443127

ABSTRACT

The effect of magnetic fields on water is still a highly controversial topic despite the vast amount of research devoted to this topic in past decades. Enhanced water evaporation in a magnetic field, however, is less disputed. The underlying mechanism for this phenomenon has been investigated in previous studies. In this paper, we present an investigation of the evaporation of water in a large gradient magnetic field. The evaporation of pure water at simulated gravity positions (0 gravity level (ab. g), 1 g, 1.56 g and 1.96 g) in a superconducting magnet was compared with that in the absence of the magnetic field. The results showed that the evaporation of water was indeed faster in the magnetic field than in the absence of the magnetic field. Furthermore, the amount of water evaporation differed depending on the position of the sample within the magnetic field. In particular, the evaporation at 0 g was clearly faster than that at other positions. The results are discussed from the point of view of the evaporation surface area of the water/air interface and the convection induced by the magnetization force due to the difference in the magnetic susceptibility of water vapor and the surrounding air.


Subject(s)
Magnetic Fields , Models, Chemical , Water/chemistry
10.
PLoS One ; 6(3): e17950, 2011 Mar 30.
Article in English | MEDLINE | ID: mdl-21479212

ABSTRACT

Protein crystals usually grow at a preferable temperature which is however not known for a new protein. This paper reports a new approach for determination of favorable crystallization temperature, which can be adopted to facilitate the crystallization screening process. By taking advantage of the correlation between the temperature dependence of the second virial coefficient (B(22)) and the solubility of protein, we measured the temperature dependence of B(22) to predict the temperature dependence of the solubility. Using information about solubility versus temperature, a preferred crystallization temperature can be proposed. If B(22) is a positive function of the temperature, a lower crystallization temperature is recommended; if B(22) shows opposite behavior with respect to the temperature, a higher crystallization temperature is preferred. Otherwise, any temperature in the tested range can be used.


Subject(s)
Crystallization/methods , Models, Chemical , Proteins/chemistry , Temperature , Animals , Chickens , Chymotrypsinogen/chemistry , Light , Muramidase/chemistry , Particle Size , Refractometry , Reproducibility of Results , Scattering, Radiation , Solutions
11.
Rev Sci Instrum ; 79(9): 093903, 2008 Sep.
Article in English | MEDLINE | ID: mdl-19044425

ABSTRACT

Containerless processing of materials is considered beneficial for obtaining high quality products due to the elimination of the detrimental effects coming from the contact with container walls. Many containerless processing methods are realized by levitation techniques. This paper describes a containerless levitation setup that utilized the magnetization force generated in a gradient magnetic field. It comprises a levitation unit, a temperature control unit, and a real-time observation unit. Known volume of liquid diamagnetic samples can be levitated in the levitation chamber, the temperature of which is controlled using the temperature control unit. The evolution of the levitated sample is observed in real time using the observation unit. With this setup, containerless processing of liquid such as crystal growth from solution can be realized in a well-controlled manner. Since the levitation is achieved using a superconducting magnet, experiments requiring long duration time such as protein crystallization and simulation of space environment for living system can be easily succeeded.


Subject(s)
Electromagnetic Phenomena , Equipment Design/instrumentation , Weightlessness , Crystallization , Muramidase/chemistry , Temperature , Water/chemistry
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