A novel method of convection compensated ENMR (CC-ENMR) has been developed
to detect electrophoretic motion of ionic species in the presence of bulk s
olution convection. This was accomplished using a gradient moment nulling t
echnique to remove spectral artifacts from heat-induced convection and usin
g the polarity switch of the applied electric field to retain spin phase mo
dulations due to electrophoretic flow. Experiments were carried out with a
mixture of 100 mM L-aspartic acid and 100 mM 4,9-dioxa-1,12-dodecanediamine
to demonstrate this new method of ENMR. CC-ENMR enhances our previously de
veloped capillary array ENMR (CA-ENMR) in solving the convection problem. T
he combined CA- and CC-ENMR approach strengthens the potential of multidime
nsional ENMR in simultaneous structural determination of coexisting protein
s and protein conformations in biological buffer solutions of high ionic st
rength. Structural mapping of interacting proteins during biochemical react
ions becomes possible in the future using ENMR techniques, which may have a
profound impact on the understanding of biological events, including prote
in folding, genetic control, and signal transduction in general. (C) 2001 A
cademic Press.