Structural dynamics of Photoactive Yellow Protein
Abstract
Photoactive Yellow Protein (PYP) is considered to be a model chromophoric protein. The dynamics of its active site during photoisomerization are considered to be a novel effect which have been looked at by several research teams around the world. Our research group designed a new time-resolved experimental system using a tunable laser and Fourier-Transform Infrared (FTIR) system in tandem. With this new experimental design we were able to analyze the active site of a Photoactive Yellow Protein mutant, N43S, during its several stages of the protein functional dynamics. Our research sets a precedent for future experimental groups hoping to utilize rapid-scan FTIR techniques to analyze PYP or other, similar chromophoric proteins.