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Precision Measurements of Binary and Multicomponent Diffusion Coefficients in Protein Solutions Relevant to Crystal Growth
 

Summary: Precision Measurements of Binary and Multicomponent Diffusion
Coefficients in Protein Solutions Relevant to Crystal Growth:
Lysozyme Chloride in Water and Aqueous NaCl at pH 4.5 and
25 C
John G. Albright,*, Onofrio Annunziata, Donald G. Miller,, Luigi Paduano,,| and
Arne J. Pearlstein
Contribution from the Chemistry Department, Texas Christian UniVersity, Fort Worth, Texas 76129,
Geosciences and EnVironmental Technologies, Lawrence LiVermore National Laboratory, P.O. Box 808,
LiVermore, California 94551, Department of Mechanical and Industrial Engineering, UniVersity of Illinois
at Urbana-Champaign, 1206 West Green Street, Urbana, Illinois 61801, and Dipartimento di Chimica,
UniVersita` di Napoli, Via Mezzocannone 4, 80134 Naples, Italy
ReceiVed October 1, 1998
Abstract: Accurate models of protein diffusion are important in a number of applications, including liquid-
liquid phase separation and growth of protein crystals for X-ray diffraction studies. In concentrated
multicomponent protein systems, significant deviations from pseudobinary behavior can be expected. Rayleigh
interferometry is used to measure the four elements (Dij)v of the ternary diffusion coefficient matrix for the
extensively investigated protein, hen egg-white lysozyme (component 1) in aqueous NaCl (component 2) at
pH 4.5 and 25 C. These are the first multicomponent diffusion coefficients measured for any protein system
at concentrations high enough to be relevant to modeling and prediction of crystal growth or other phase
transitions, and the first for a system involving lysozyme at any concentration. The four ternary diffusion

  

Source: Annunziata, Onofrio - Department of Chemistry, Texas Christian University

 

Collections: Chemistry