Increasing the accuracy of exchange parameters reporting on slow dynamics by performing CEST experiments with 'high' B fields.

Over the last decade chemical exchange saturation transfer (CEST) NMR methods have emerged as powerful tools to characterize biomolecular conformational dynamics occurring between a visible major state and 'invisible' minor states. The ability of the CEST experiment to detect these minor states, and provide precise exchange parameters, hinges on using appropriate B field strengths during the saturation period. Typically, a pair of B fields with ω (=2πB) values around the exchange rate k are chosen.

Studying micro to millisecond protein dynamics using simple amide N CEST experiments supplemented with major-state R and visible peak-position constraints.

Over the last decade amide N CEST experiments have emerged as a popular tool to study protein dynamics that involves exchange between a 'visible' major state and sparsely populated 'invisible' minor states. Although initially introduced to study exchange between states that are in slow exchange with each other (typical exchange rates of, 10 to 400 s), they are now used to study interconversion between states on the intermediate to fast exchange timescale while still using low to moderate (5 to 350 Hz) 'saturating' B fields. The N CEST experiment is very sensitive to exchange as the exchange delay T can be quite long (~0.