Designer amphiphilic short peptides enhance thermal stability of isolated photosystem-I.

ABSTRACT: Stability of membrane protein is crucial during protein purification and crystallization as well as in the fabrication of protein-based devices. Several recent studies have examined how various surfactants can stabilize membrane proteins out of their native membrane environment. However, there is still no single surfactant that can be universally employed for all membrane proteins. Because of the lack of knowledge on the interaction between surfactants and membrane proteins, the choice of a surfactant for a specific membrane protein remains purely empirical. Here we report that a group of short amphiphilic peptides improve the thermal stability of the multi-domain protein complex photosystem-I (PS-I) in aqueous solution and that the peptide surfactants have obvious advantages over other co

SUBMITTER: Ge B 

PROVIDER: S-EPMC2858086 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature