Quantification of binary diffusion in protein crystals.

Aleksandar Cvetkovic; Cristian Picioreanu; Adrie J J Straathof; Rajamani Krishna; Luuk A M van der Wielen

doi:10.1021/jp050289c

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Quantification of binary diffusion in protein crystals.

Aleksandar Cvetkovic·Cristian Picioreanu·Adrie J J Straathof·Rajamani Krishna·Luuk A M van der Wielen

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Abstract

The use of confocal laser scanning microscopy for visualization and quantification of binary diffusion within anisotropic porous material is described here for the first time. The dynamics of adsorption profiles of dianionic fluorescein, zwitterionic rhodamine B, and their mixture in the cationic native orthorhombic lysozyme crystal were subsequently analyzed. All data could be described by a classical pore diffusion model. There was no change in the adsorption characteristics, but diffusion decreased with the introduction of a second solute in the solution. It was found that diffusion is determined by the combination of steric and electrostatic interactions,while adsorption is dependent on electrostatic and hydrophobic interactions. Thus, it was established that the outcome of binary transport depends on the solute, protein, and crystal characteristics.

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Adsorption Animals Anisotropy Biological Transport Biophysics Cations Chemistry, Physical Crystallization Diffusion Microscopy, Confocal Muramidase Proteins Rhodamines Solutions Static Electricity Journal Article Research Support, Non-U.S. Gov't

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Aleksandar Cvetkovic, Cristian Picioreanu, Adrie J J Straathof, Rajamani Krishna, Luuk A M van der Wielen. 2005-06-02. Quantification of binary diffusion in protein crystals.. https://doi.org/10.1021/jp050289c

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