Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformations.

ABSTRACT: Proteins may undergo multiple conformational changes required for their function. One strategy used to estimate target-site positions in unknown structural conformations involves single-pair resonance energy transfer (RET) distance measurements. However, interpretation of inter-residue distances is difficult when applied to three-dimensional structural rearrangements, especially in homomeric systems. We developed a positioning method using inverse trilateration/triangulation to map target sites within a homomeric protein in all defined states, with simultaneous functional recordings. The procedure accounts for probe diffusion to accurately determine the three-dimensional position and confidence region of lanthanide LRET donors attached to a target site (one per subunit), relative to a sing

SUBMITTER: Hyde HC 

PROVIDER: S-EPMC3633233 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature