Computer simulation of proteins: Adsorption, gelation and self-association

The continued application of computer simulation techniques to the study of protein conformation promises to throw light on their role as functional ingredients in food systems. This review concentrates on three areas where protein structure impacts on functionality in food systems, namely protein adsorption at a surface, gelation and self-association. Recent studies have demonstrated that adsorbed proteins do not take up a unique conformation at an interface, but can access a range of conformations that are close to the global energy minimum. More detailed simulations have also highlighted the changes in secondary structure that may occur on adsorption, particularly the possibility of intra-molecular ß-sheet formation. Studies have also investigated the importance of intra-molecular ß-sheet in the formation of amyloid fibrils, a process that may be relevant to the formation of fine-stranded whey protein food gels. Significant progress has also been made in the simulation of micellization and mesophase formation in blocks copolymer solutions, and the application of these methods to the study of milk casein self-association. Ultimately, it is believed this will give insight into the structure and formation of the casein micelle. © 2004 Elsevier Ltd. All rights reserved.