A case study of thermostability in phycobiliproteins using algorithm recurrence quantification analysis

摘要

The basis for resistance to denaturation in thermophilic proteins has been a subject of interest for many years. A comparitive study of the properties of thermophilic proteins as those with those of the less stable counterparts from mesophilic organisms can provide an insight to as how nature adapts a protein structure to extreme environmental conditions and this information can be used in protein engineering to make more stable proteins by chemical modification or site directed mutagenesis. Since cyanobacteria exsist in a diverse ecological niches and consequently thrive under vastly different environmental stress, their major protein, phycocyanin is an ideal probe in investigating the thermostability of proteins.