NMR Experiments
NMR Methods to measure proton chemical exchange rates in proteins generally requires
the acquisition of
multidimensional heteronuclear inverse NMR experiments in H2O:
- Conventional saturation transfer experiments in where a 2D 15N HSQC experiment correlation spectrum is acquired without presaturation and compared with one with 3-4 seconds of presaturation:
- Water-selective 2D inverse experiments
-
MEXICO (
93JACS11620
,
95JB306
)
-
Relaxation-compensated 1H-15N CPMG experiment (
99JACS2331
)
to measure chemical or conformational exchange time constants from 0.5
to 5 ms
- Characterization of chemical exchange in large proteins by TROSY techniques
(
05METH430
)