Chromophore packing leads to hysteresis in GFP.

ABSTRACT: Green fluorescent protein (GFP) possesses a unique folding landscape with a dual basin leading to the hysteretic folding behavior observed in experiment. While theoretical data do not have the resolution necessary to observe details of the chromophore during refolding, experimental results point to the chromophore as the cause of the observed hysteresis. With the use of NMR spectroscopy, which probes at the level of the individual residue, the hysteretic intermediate state is further characterized in the context of the loosely folded isomerized native-like state {N(iso)} predicted in simulation. In the present study, several residues located in the lid of GFP indicate heterogeneity of the native states. Some of these residues show chemical shifts when the native-like intermediate {N(iso)}

SUBMITTER: Andrews BT 

PROVIDER: S-EPMC3566660 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature