ABSTRACT
The (dis)orderly aggregation of lysozyme is an intense field of research nowadays since such a model system contains all necessary paradigms to solve, preventing this way from the as yet applied trial-and-error method for obtaining the desired crystalline and other forms of lysozyme aggregates. The notions of nucleation-growth phase change, combined properly with the so-called viscoelastic phase separation, and opened toward its thermodynamic-kinetic, generally non-Markovian character, may improve considerably the overall description of the process against the impractical trialand-error method. Both, seemingly simplified stochastic-in-nature analyses, carried out at a mesoscopic level, supported suitably Synchrotron Radiation and Structural Proteomics Edited by Eugenia Pechkova and Christian Riekel Copyright © 2012 Pan Stanford Publishing Pte. Ltd. www.panstanford.com
by submesoscopic-level computer simulations of this interface-controlled crystal formation process, may remedy and foster further actions toward more sophisticated and efficient solution to this long-standing, truly complex phase change and/or phase separation involving puzzle, both of them dealt with inseparably, what stands for a certain appreciable novelty of the present study. A final message that comes from the offered study so far states that a type of hybrid model combining sensitively some parts of analytical analyses with some well-designed computer simulation complementary co-analysis can assure a distinctive progress toward solving practically many of systems of interest. 5.1 INTRODUCTIONProtein molecules are made up of amino acids and possess amphiphilic nature when subjected to solvent, especially to water. Lysozyme is one protein molecule commonly met in nature and very prone to crystallize. The obtained crystals, depending on a broad spectrum of crystal formation conditions, have, in general, polymorphic character, expressed in terms of its unit cell, and its alterations: they are often termed non-Kossel crystals what makes them distinguishable from standard NaCl-type crystal forms.Biologically motivated modeling becomes recently a necessary activity taken up by physicists toward obtaining first quantitative information about complex biosystems to be dealt with. Protein systems are those that are presently of central interest from the statistical mechanical and non-equilibrium thermodynamics points of view since they conform to basic research tasks underwent by both subdisciplines of statistical condensed matter physics (Basu and Chowdhury, 2007).
