<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Cardo L</dc:creator>
  <dc:creator>Karunatilaka KS</dc:creator>
  <dc:creator>Rueda D</dc:creator>
  <dc:creator>Sigel RK</dc:creator>
  <dc:date>2012</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">A procedure to investigate the folding of group II intron by single molecule Fluorescence Resonance Energy Transfer (smFRET) using total internal reflection fluorescence microscopy (TIRFM) is described in this chapter. Using our previous studies on the folding and dynamics of a large ribozyme in the presence of metal ions (i.e., Mg(2+) and Ca(2+)) and/or the DEAD-box protein Mss116 as an example, we here describe step-by-step procedures to perform experiments. smFRET allows the investigation of individual molecules, thus, providing kinetic and mechanistic information hidden in ensemble averaged experiments.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/65865</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1007/978-1-61779-545-9_15</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/22315073</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Methods in molecular biology (Clifton, N.J.). - 2012</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Base Sequence</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Calibration</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">DEAD-box RNA Helicases</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Fluorescence Polarization</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Fluorescence Resonance Energy Transfer</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Introns</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Magnesium Chloride</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Microfluidic Analytical Techniques</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Molecular Sequence Data</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Nucleic Acid Conformation</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Polyethylene Glycols</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">RNA, Catalytic</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Saccharomyces cerevisiae</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Saccharomyces cerevisiae Proteins</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Transcription, Genetic</dc:subject>
  <dc:title xmlns:ns16="xml" ns16:lang="en">Single molecule FRET characterization of large ribozyme folding.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
