
<oai_dc:dc xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" 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:title>Some Relationships of Structure to Function in Ribonuclease</dc:title>
  <dc:subject>Ribonucleases</dc:subject>
  <dc:subject>Oxidation-Reduction</dc:subject>
  <dc:subject>Protein Conformation</dc:subject>
  <dc:subject>Disulfides</dc:subject>
  <dc:description>This study by White and Anfinsen on the renaturation of fully denatured ribonuclease, or RNase, required subsequent supporting investigations to establish what came to be called the &quot;thermodynamic hypothesis.&quot;  Here they reported that RNase activity depended upon a variety of structural features, but noted that it could be inferred from the results of their experimentation that only a small part of the enzyme molecule, what they termed the &quot;active center,&quot; was necessary for catalyst.</dc:description>
  <dc:publisher>New York Academy of Sciences, 4 September 1959</dc:publisher>
  <dc:publisher>The New York Academy of Sciences, 4 September 1959</dc:publisher>
  <dc:contributor>Annals of the New York Academy of Sciences</dc:contributor>
  <dc:contributor>White, F. H., Jr</dc:contributor>
  <dc:contributor>Anfinsen, Christian B.</dc:contributor>
  <dc:contributor>Anfinsen, Christian B.</dc:contributor>
  <dc:type>Articles</dc:type>
  <dc:format>Archival Materials</dc:format>
  <dc:format>Text</dc:format>
  <dc:format>9 pages</dc:format>
  <dc:identifier>nlm:nlmuid-101584571X166-doc</dc:identifier>
  <dc:identifier>101584571X166</dc:identifier>
  <dc:identifier>http://resource.nlm.nih.gov/101584571X166</dc:identifier>
  <dc:identifier>Profiles ID: KKBBKY</dc:identifier>
  <dc:language>English</dc:language>
  <dc:relation>Profiles in Science</dc:relation>
</oai_dc:dc>
