Measurement of ¹⁵N relaxation rates in perdeuterated proteins by TROSY-based methods.

ABSTRACT: While extracting dynamics parameters from backbone (15)N relaxation measurements in proteins has become routine over the past two decades, it is increasingly recognized that accurate quantitative analysis can remain limited by the potential presence of systematic errors associated with the measurement of (15)N R(1) and R(2) or R(1ρ) relaxation rates as well as heteronuclear (15)N-{(1)H} NOE values. We show that systematic errors in such measurements can be far larger than the statistical error derived from either the observed signal-to-noise ratio, or from the reproducibility of the measurement. Unless special precautions are taken, the problem of systematic errors is shown to be particularly acute in perdeuterated systems, and even more so when TROSY instead of HSQC elements are used to r

SUBMITTER: Lakomek NA 

PROVIDER: S-EPMC3412688 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature