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Time Evolution of Crystallization Phase of Lysozyme Protein in Aqueous Salt Solution as Studied by Scattering Techniques by S. Chodankar; V.K. Aswal; J. Kohlbrecher; P.A. Hassan; A.G. Wagh is a Physics and Astronomy article available to read on EtoBox.

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Formation of protein crystallization in 1 wt% lysozyme in aqueous solution has been studied as a function of salt (KBr) concentration. The onset and the rate of crystallization in this protein solution strongly depend on the KBr concentration. It is found, while the presence of 0.4 M KBr starts producing crystals in 1 h, it takes about 120 h for 0.2 M KBr. The rate of protein crystallization has been studied by small-angle neutron scattering (SANS) and dynamic light scattering (DLS) in 1 wt% lysozyme solution in presence of three different KBr concentrations 0.3, 0.26 and 0.24 M, which show the start of crystallization at about 1.5, 3 and 5 h, respectively. Measurements have been performed for every half an hour from freshly prepared protein sample up to 72 h. Both time-evolved SANS and DLS data have been used to calculate the fraction of crystallization as a function of time. The variation of crystallization with time shows three distinguished regions: (i) prior to and the beginning of crystallization, which shows no significant change in the crystallization, (ii) growth region showing a significant increase in the crystallization with time and (iii) saturation region. These three

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Author

S. Chodankar; V.K. Aswal; J. Kohlbrecher; P.A. Hassan; A.G. Wagh

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0921-4526)

Published

2007

Language

EN

Field

Physics and Astronomy (Physical Sciences)