RNA-protein recognition is a crucial aspect of many biological processes that still remains relatively poorly understood at the structural and thermodynamic level. NMR studies on RNA-protein complexes have been limited to a qualitative description of sites of interactions through mapping of chemical shift changes upon complex formation Two major inconvenients are their limited solubility and high molecualr weight.

General reading: 00METH198 , 00COP53 , 01METH357 and 05METH525

NMR Experiments

NMR Chemical shift perturbation analysis

Intermolecular NOEs

Protein Deuteration

Use of paramagnetic spin labels

Residual Dipolar Couplings

Some examples in the bibliography:

U1A protein / RNA polyadenylation inhibition element ( 98JB59-11 )

Human U1A protein / RNA complexes ( 99JMB967-294