Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions.

ABSTRACT: The structure and dynamics of proteins underlies the workings of virtually every biological process. Existing biophysical methods are inadequate to measure protein structure at atomic resolution, on a rapid time scale, with limited amounts of protein, and in the context of a cell or membrane. FRET can measure distances between two probes, but depends on the orientation of the probes and typically works only over long distances comparable with the size of many proteins. Also, common probes used for FRET can be large and have long, flexible attachment linkers that position dyes far from the protein backbone. Here, we improve and extend a fluorescence method called transition metal ion FRET that uses energy transfer to transition metal ions as a reporter of short-range distances in proteins w

SUBMITTER: Taraska JW 

PROVIDER: S-EPMC2741476 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature