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Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

Kavak Balci, Gulten


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<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>Kavak Balci, Gulten</dc:creator>
  <dc:date>2021-01-01</dc:date>
  <dc:description>In this work, the proton spin-lattice (T-1) and spin-spin (T-2) relaxation times of aqueous solutions of bovine serum albumin (BSA) were investigated as a function of temperature. The T-1 relaxation times were measured versus temperature (T) for five H2O solutions containing different BSA concentrations. The sample temperature was varied from 304 to 253 K for each concentration. T-2 measurements were carried out versus the BSA concentrations only. The least-square fitting of ln(T-1) versus T-1 yields a linear correlation. The effective correlation times tau(1) for T-1 and tau(2) for T-2 were calculated by using experimental data and the related theory. The data suggest that surface water is responsible for the dipolar relaxation mechanisms. Both T-1 and T-2 mechanisms are caused by overall tumbling of albumin molecule causing the rotational correlation time. However, some slow motions may contribute to the T-2 mechanism.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/236362</dc:identifier>
  <dc:identifier>oai:aperta.ulakbim.gov.tr:236362</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>JOURNAL OF SOLUTION CHEMISTRY 50(2) 232-239</dc:source>
  <dc:title>Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
</oai_dc:dc>
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