Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain.

ABSTRACT: Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suffers from limited signal-to-noise, signal overlap, and a need for fractional ¹³C or ²H labeling. Here we introduce a simple strategy measuring initial ¹H relaxation rates during a ¹H TOCSY sequence like DIPSI-2, which can be appended to the beginning of any multi-dimensional NMR sequence that begins on ¹H. The TOCSY RF field compels all ¹H atoms to behave similarly under the influence of strong coupling and rotating frame cross-relaxation, so that differences in relaxation rates are due pri

SUBMITTER: Danmaliki GI 

PROVIDER: S-EPMC9427894 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature