Ionic conductivity, transference numbers, composition and mobility of ions in cross-linked lysozyme crystals

Morozova, Tamara Ya.; Качалова, Г.С.; Lanina, N. F.; Evtodienko, V.U.; Botin, A.S.; Shlyapnikova, Elena A.; Морозов, В. Н.

doi:10.1016/0301-4622(96)00007-5

Cited by 18 publications

(28 citation statements)

References 23 publications

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“…During the experiments, there was no swelling of the crystals according to observations by Leica TCS SP confocal microscopy (Cvetkovic et al, 2004). These findings are in agreement with the literature (Morozova et al, 1996).…”

Section: Cross-linked Tetragonal Crystals: Influence Of Mops Concentrsupporting

confidence: 87%

Adsorption of fluorescein by protein crystals

Cvetkovic

Zomerdijk

Straathof

et al. 2004

Biotech & Bioengineering

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Adsorption characteristics of native and cross-linked lysozyme crystals were examined using fluorescein as model adsorbate. The adsorption isotherms exhibited Langmuir or linear behavior. The affinity constant (b1) and the adsorption capacity (Qsat) for fluorescein were found to depend on the type and concentration of co-solute present in the solution. The dynamics of adsorption isotherm transition from Langmuir to linear showed that affinity of lysozyme for solutes increases in the order 2-(cyclohexylamino)ethanesulphonic acid (CHES), 4-morpholinepropanesulphonic acid (MOPS), acetate, fluorescein. Furthermore, the crystal morphology, the degree of cross-linking of the crystals, and, in particular, solution pH were identified as factors determining fluorescein adsorption by the lysozyme crystals. These factors seem to affect crystal capacity for the solute more than affinity for the solute. Adsorption of fluorescein by cross-linked tetragonal lysozyme crystals was exponentially dependent on the lysozyme net charge calculated from the final solution pH. The 3-5-fold increase in the fluorescein adsorption as a result of cross-linking is presumably due to the increasing hydrophobicity of the lysozyme crystal.

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Section: Cross-linked Tetragonal Crystals: Influence Of Mops Concentrsupporting

confidence: 87%

Adsorption of fluorescein by protein crystals

Cvetkovic

Zomerdijk

Straathof

et al. 2004

Biotech & Bioengineering

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“…Some of the features related to ion transport through ion channels in biomembranes can be obtained by looking at a protein pore in protein crystals and vice versa [11,26]. They are made from the same protein constituents; their crosssections change along the pore axes and their conductivities are comparable.…”

Section: S525mentioning

confidence: 99%

“…This pore seems more like a series of pocket cavities. Such a pore is not remarkable as a diffusion channel, but could be considered for studying the diffusion anisotropy [11,14,16]. Figure 1(b) shows a 2 × 2 × 2 βLG lattice.…”

Section: Calculationsmentioning

confidence: 99%

“…Understanding the nature of transport of small molecules and ions through βLG crystals is essential in practical applications of this protein crystal either as a porous separation medium or as a (bio)catalyst [7,16]. Because of the similarities between channels in protein crystals and in biological membranes, and the much greater precision with which the atomic structure and properties of many protein crystals are known from x-ray studies, protein crystals serve as a suitable model for studying diffusion of ions and small molecules in biological channels, and simulations for protein crystals provide new insights into diffusion in biological channels in a general sense as well [11,14,26]. Both the water-βLG and ion-βLG interactions were studied experimentally [27,28].…”

Section: Introductionmentioning

confidence: 99%

“…This property was initially used in preparation of isomorphous derivatives in protein crystallography [6,10]. Several studies have focused on the experimental determination of the solute and water transport in protein crystals [11][12][13][14]. Some reliable experimentally based diffusion models have been proposed recently [15].…”

Section: Introductionmentioning

confidence: 99%

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Diffusion of water and sodium counter-ions in nanopores of a β-lactoglobulin crystal: a molecular dynamics study

Malek¹,

Odijk²,

Coppens³

2005

Nanotechnology

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The dynamics of water and sodium counter-ions (Na + ) in a C222 1 orthorhombic β-lactoglobulin crystal is investigated by means of 5 ns molecular dynamics simulations. The effect of the fluctuation of the protein atoms on the motion of water and sodium ions is studied by comparing simulations in a rigid and in a flexible lattice. The electrostatic interactions of sodium ions with the positively charged LYS residues inside the crystal channels significantly influence the ionic motion. According to our results, water molecules close to the protein surface undergo an anomalous diffusive motion. On the other hand, the motion of water molecules further away from the protein surface is normal diffusive. Protein fluctuations affect the diffusion constant of water, which increases from 0.646 ± 0.108 to 0.887 ± 0.41 nm 2 ns −1 , when protein fluctuations are taken into account. The pore size (0.63-1.05 nm) and the water diffusivities are in good agreement with previous experimental results. The dynamics of sodium ions is disordered. LYS residues inside the pore are the main obstacles to the motion of sodium ions. However, the simulation time is still too short for providing a precise description of anomalous diffusion of sodium ions. The results are not only of interest for studying ion and water transport through biological nanopores, but may also elucidate water-protein and ion-protein interactions in protein crystals.

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Quantifying anisotropic solute transport in protein crystals using 3‐D laser scanning confocal microscopy visualization

Cvetkovic

Straathof

Hanlon³

et al. 2004

Biotech & Bioengineering

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The diffusion of a solute, fluorescein into lysozyme protein crystals has been studied by confocal laser scanning microscopy (CLSM). Confocal laser scanning microscopy makes it possible to non-invasively obtain high-resolution three-dimensional (3-D) images of spatial distribution of fluorescein in lysozyme crystals at various time steps. Confocal laser scanning microscopy gives the fluorescence intensity profiles across horizontal planes at several depths of the crystal representing the concentration profiles during diffusion into the crystal. These intensity profiles were fitted with an anisotropic model to determine the diffusivity tensor. Effective diffusion coefficients obtained range from 6.2 x 10(-15) to 120 x 10(-15) m2/s depending on the lysozyme crystal morphology. The diffusion process is found to be anisotropic, and the level of anisotropy depends on the crystal morphology. The packing of the protein molecules in the crystal seems to be the major factor that determines the anisotropy.

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Ionic conductivity, transference numbers, composition and mobility of ions in cross-linked lysozyme crystals

Cited by 18 publications

References 23 publications

Adsorption of fluorescein by protein crystals

Adsorption of fluorescein by protein crystals

Diffusion of water and sodium counter-ions in nanopores of a β-lactoglobulin crystal: a molecular dynamics study

Quantifying anisotropic solute transport in protein crystals using 3‐D laser scanning confocal microscopy visualization

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