Literature DB >> 18982287

Monitoring assembly of ribonucleoprotein complexes by isothermal titration calorimetry.

Michael I Recht1, Sean P Ryder, James R Williamson.   

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.

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Year:  2008        PMID: 18982287      PMCID: PMC2922068          DOI: 10.1007/978-1-60327-475-3_8

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  13 in total

1.  Exact analysis of competition ligand binding by displacement isothermal titration calorimetry.

Authors:  B W Sigurskjold
Journal:  Anal Biochem       Date:  2000-01-15       Impact factor: 3.365

Review 2.  Direct measurement of protein binding energetics by isothermal titration calorimetry.

Authors:  S Leavitt; E Freire
Journal:  Curr Opin Struct Biol       Date:  2001-10       Impact factor: 6.809

3.  Central domain assembly: thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex.

Authors:  M I Recht; J R Williamson
Journal:  J Mol Biol       Date:  2001-10-12       Impact factor: 5.469

Review 4.  Applications of calorimetric methods to drug discovery and the study of protein interactions.

Authors:  Patricia C Weber; F Raymond Salemme
Journal:  Curr Opin Struct Biol       Date:  2003-02       Impact factor: 6.809

Review 5.  Kinetic studies of RNA-protein interactions using surface plasmon resonance.

Authors:  Phinikoula S Katsamba; Sungmin Park; Ite A Laird-Offringa
Journal:  Methods       Date:  2002-02       Impact factor: 3.608

6.  Theoretical aspects of isothermal titration calorimetry.

Authors:  L Indyk; H F Fisher
Journal:  Methods Enzymol       Date:  1998       Impact factor: 1.600

7.  Calculation of protein extinction coefficients from amino acid sequence data.

Authors:  S C Gill; P H von Hippel
Journal:  Anal Biochem       Date:  1989-11-01       Impact factor: 3.365

8.  Synthesis of small RNAs using T7 RNA polymerase.

Authors:  J F Milligan; O C Uhlenbeck
Journal:  Methods Enzymol       Date:  1989       Impact factor: 1.600

9.  Rapid measurement of binding constants and heats of binding using a new titration calorimeter.

Authors:  T Wiseman; S Williston; J F Brandts; L N Lin
Journal:  Anal Biochem       Date:  1989-05-15       Impact factor: 3.365

10.  Folding of A+U-rich RNA elements modulates AUF1 binding. Potential roles in regulation of mRNA turnover.

Authors:  G M Wilson; K Sutphen; G Brewer
Journal:  J Biol Chem       Date:  2000-12-21       Impact factor: 5.157

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  3 in total

1.  Studying RNA-RNA and RNA-protein interactions by isothermal titration calorimetry.

Authors:  Andrew L Feig
Journal:  Methods Enzymol       Date:  2009       Impact factor: 1.600

2.  A rapid method for assessing the RNA-binding potential of a protein.

Authors:  K Bendak; F E Loughlin; V Cheung; M R O'Connell; M Crossley; J P Mackay
Journal:  Nucleic Acids Res       Date:  2012-04-03       Impact factor: 16.971

3.  ARE-mediated decay controls gene expression and cellular metabolism upon oxygen variations.

Authors:  Bérengère de Toeuf; Romuald Soin; Abdelkarim Nazih; Marija Dragojevic; Dukas Jurėnas; Nadège Delacourt; Long Vo Ngoc; Abel Garcia-Pino; Véronique Kruys; Cyril Gueydan
Journal:  Sci Rep       Date:  2018-03-26       Impact factor: 4.379

  3 in total

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