Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus.

ABSTRACT: Biological processes occur in complex environments containing a myriad of potential interactors. Unfortunately, limitations on the sensitivity of biophysical techniques normally restrict structural investigations to purified systems, at concentrations that are orders of magnitude above endogenous levels. Dynamic nuclear polarization (DNP) can dramatically enhance the sensitivity of nuclear magnetic resonance (NMR) spectroscopy and enable structural studies in biologically complex environments. Here, we applied DNP NMR to investigate the structure of a protein containing both an environmentally sensitive folding pathway and an intrinsically disordered region, the yeast prion protein Sup35. We added an exogenously prepared isotopically labeled protein to deuterated lysates, rendering the bio

SUBMITTER: Frederick KK 

PROVIDER: S-EPMC4621972 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature