Detail Analysis for Energy Transfer and Pigment Assembling in C−Phycocyanin through Time−Resolved Spectroscopy and AlphaFold2

Abstract

The time-resolved fluorescence spectroscopy of the C−phycocyanin (C−PC) complex from the cyanobacterium Spirulina platensis (S. platensis) hexamer with the sub-picosecond resolution was detected, and the energy transfer pathways and related transfer rates were identified through the multiexponential analysis based on Monte-Carlo method. With the purpose to construct the relationship between the functions and the structure in vivo, the three−dimension (3D) protein structure was predicted via AlphaFold2, and the arrangement of chromophores treated as the energy transfer nodes were obtained. The experiment results have been matched well with the structure prediction. This work suggests a new way to investigate structure prediction in vivo and the corresponding functions.

Keywords

• C-phycocyanin
• AlphaFold2
• energy transfer
• time-resolved