Tethered spectroscopic probes estimate dynamic distances with subnanometer resolution in voltage-dependent potassium channels.

ABSTRACT: Measurements of inter- and intramolecular distances are important for monitoring structural changes and understanding protein interaction networks. Fluorescence resonance energy transfer and functionalized chemical spacers are the two predominantly used strategies to map short-range distances in living cells. Here, we describe the development of a hybrid approach that combines the key advantages of spectroscopic and chemical methods to estimate dynamic distance information from labeled proteins. Bifunctional spectroscopic probes were designed to make use of adaptable-anchor and length-varied spacers to estimate molecular distances by exploiting short-range collisional electron transfer. The spacers were calibrated using labeled polyproline peptides of defined lengths and validated by molec

SUBMITTER: Jarecki BW 

PROVIDER: S-EPMC3882458 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature