| Literature DB >> 20713011 |
Ronald Gebhardt1, Eugenia Pechkova, Christian Riekel, Claudio Nicolini.
Abstract
The formation of thaumatin crystals by Langmuir-Blodgett (LB) film nanotemplates was studied by the hanging-drop technique in a flow-through cell by synchrotron radiation micrograzing-incidence small-angle x-ray scattering. The kinetics of crystallization was measured directly on the interface of the LB film crystallization nanotemplate. The evolution of the micrograzing-incidence small-angle x-ray scattering patterns suggests that the increase in intensity in the Yoneda region is due to protein incorporation into the LB film. The intensity variation suggests several steps, which were modeled by system dynamics based on first-order differential equations. The kinetic data can be described by two processes that take place on the LB film, a first, fast, process, attributed to the crystal growth and its detachment from the LB film, and a second, slower process, attributed to an unordered association and conversion of protein on the LB film. 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID: 20713011 PMCID: PMC2920630 DOI: 10.1016/j.bpj.2010.03.068
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033