Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules.

ABSTRACT: Exchange between conformational states is required for biomolecular catalysis, allostery, and folding. A variety of NMR experiments have been developed to quantify motional regimes ranging from nanoseconds to seconds. In this work, we describe an approach to speed up the acquisition of chemical exchange saturation transfer (CEST) experiments that are commonly used to probe millisecond to second conformational exchange in proteins and nucleic acids. The standard approach is to obtain CEST datasets through the acquisition of a series of 2D correlation spectra where each experiment utilizes a single saturation frequency to ¹H, ¹⁵N or ¹³C. These pseudo 3D datasets are time consuming to collect and are further lengthened by reduced signal to noise stemming from

SUBMITTER: Leninger M 

PROVIDER: S-EPMC5989009 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature