title: Monitoring assembly of ribonucleoprotein complexes by isothermal titration calorimetry.
abstract: Isothermal titration calorimetry (ITC) is a useful technique to study RNA-protein interactions as it provides the only method by which the thermodynamic parameters of free energy, enthalpy, and entropy can be directly determined. This chapter presents a general procedure for studying RNA-protein interactions using ITC and gives specific examples for monitoring the binding of Caenorhabditis elegans GLD-1 STAR domain to TGE RNA and the binding of Aquifex aeolicus S6:S18 ribosomal protein heterodimer to an S15-ribosomal RNA complex.
authors.affiliation: Palo Alto Research Center, Palo Alto, California, USA.
authors.forename: Michael I
authors.initials: MI
authors.lastname: Recht
authors.forename: Sean P
authors.initials: SP
authors.lastname: Ryder
authors.forename: James R
authors.initials: JR
authors.lastname: Williamson
mesh_terms: D002151:Calorimetry / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D011506:Proteins; D012261:Ribonucleoproteins; D012313:RNA