RNA folds into complex structures that can interact specifically with effec
tor proteins. These interactions are essential for various biological funct
ions. In order to discover small molecules that can affect important RNA-pr
otein complexes, a thorough analysis of the thermodynamics and kinetics of
RNA-protein binding is required. This can facilitate the formulation of hig
h-throughput screening strategies and the development of structure-activity
relationships for compound leads. In addition to traditional methods, such
as filter binding, gel mobility shift assay and various fluorescence techn
iques, newer methods such as surface plasmon resonance and mass spectrometr
y are being used for the study of RNA-protein interactions.