Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.

ABSTRACT: A mathematico-physically valid formulation is required to infer properties of disordered protein conformations from single-molecule Förster resonance energy transfer (smFRET). Conformational dimensions inferred by conventional approaches that presume a homogeneous conformational ensemble can be unphysical. When all possible-heterogeneous as well as homogeneous-conformational distributions are taken into account without prejudgment, a single value of average transfer efficiency 〈E〉 between dyes at two chain ends is generally consistent with highly diverse, multiple values of the average radius of gyration 〈R_g〉. Here we utilize unbiased conformational statistics from a coarse-grained explicit-chain model to establish a general logical framework to quantify this fundamental ambigui

SUBMITTER: Song J 

PROVIDER: S-EPMC5658725 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature